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{ "PMID": 23, "DateCompleted": { "Year": 1976, "Month": 1, "Day": 26 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2020, "Month": 2, "Day": 25 }, "Article": { "Abstract": { "AbstractText": "The distribution of blood flow to the subendocardial, medium and subepicardial layers of the left ventricular free wall was studied in anaesthetized dogs under normoxic (A), hypoxic (B) conditions and under pharmacologically induced (etafenone) coronary vasodilation (C). Regional myocardial blood flow was determined by means of the particle distribution method. In normoxia a transmural gradient of flow was observed, with the subendocardial layers receiving a significantly higher flow rate compared with the subepicardial layers. In hypoxia induced vasodilation this transmural gradient of flow was persistent. In contrast a marked redistribution of regional flow was observed under pharmacologically induced vasodilation. The transmural gradient decreased. In contrast to some findings these experiments demonstrate that a considerable vasodilatory capacity exists in all layers of the myocardium and can be utilized by drugs. The differences observed for the intramural distribution pattern of flow under hypoxia and drug induced vasodilation support the hypothesis that this pattern reflects corresponding gradients of regional myocardial metabolism." }, "ArticleTitle": "Effect of etafenone on total and regional myocardial blood flow.", "AuthorList": { "Author": { "LastName": [ "Flohr", "Breull" ], "ForeName": [ "H", "W" ], "Initials": [ "H", "W" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "G0700399" ], "Agency": [ "Medical Research Council" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "Germany" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "142M471B3J", "S88TT14065" ], "NameOfSubstance": [ "Propiophenones", "Vasodilator Agents", "Carbon Dioxide", "Oxygen" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Animals", "Blood Pressure", "Carbon Dioxide", "Cardiac Output", "Coronary Circulation", "Coronary Vessels", "Dogs", "Heart Rate", "Heart Septum", "Heart Ventricles", "Hydrogen-Ion Concentration", "Hypoxia", "Oxygen", "Propiophenones", "Vasodilator Agents" ], "QualifierName": [ "", "drug effects", "blood", "drug effects", "drug effects", "drug effects", "", "drug effects", "", "", "", "physiopathology", "blood", "pharmacology", "pharmacology" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "23" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 9, 9, 9 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 30, "DateCompleted": { "Year": 1976, "Month": 2, "Day": 13 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2020, "Month": 2, "Day": 25 }, "Article": { "Abstract": { "AbstractText": "Seven distinct glycosidases (EC 3.2) have been characterized in guinea-pig epidermis. Their properties indicate them to be of lysosomal origin. The 'profile' of the epidermal glycosidases is significantly different from that reported for whole skin, the activities of beta-galactosidase and beta-acetylglucosaminidase being very high and those of the remaining enzymes relatively low in epidermis." }, "ArticleTitle": "Lysosomal hydrolases of the epidermis. I. Glycosidases.", "AuthorList": { "Author": { "LastName": [ "Mier", "van den Hurk" ], "ForeName": [ "P D", "J J" ], "Initials": [ "PD", "JJ" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "MC_UP_A620_1017" ], "Agency": [ "Medical Research Council" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "EC 3.2.1.-", "EC 3.2.1.-", "EC 3.2.1.52" ], "NameOfSubstance": [ "Galactosidases", "Glycoside Hydrolases", "Acetylglucosaminidase" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Acetylglucosaminidase", "Animals", "Galactosidases", "Glycoside Hydrolases", "Guinea Pigs", "Hydrogen-Ion Concentration", "Kinetics", "Lysosomes", "Skin" ], "QualifierName": [ "metabolism", "", "metabolism", "metabolism", "", "", "", "enzymology", "enzymology" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "30", "10.1111/j.1365-2133.1975.tb06468.x" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 7, 7, 7 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 73, "DateCompleted": { "Year": 1976, "Month": 2, "Day": 13 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 6, "Day": 9 }, "Article": { "Abstract": { "AbstractText": "1. Based on incorporation of radioactively labeled N-ethylmaleimide, the readily reactive thiol groups of isolated myosin (EC 3.6.1.3) from fast, slow and cardiac muscles could be classified into 3 types. All 3 myosins contain 2 thiol-1, 2 thiol-2 and a variable number of thiol-3 groups per molecule. Both thiol-1 and thiol-2 groups which are essential for functioning of the K+-stimulated ATPase, are located in the heavy chains in all 3 myosin types. 2. The variation in the incorporation pattern of N-ethylmaleimide over the 3 thiol group classes under steady-state conditions of Mg(2+) - ATP hydrolysis allowed different conformations of some reaction intermediates to be characterized. In all 3 types of myosin the hydrolytic cycle of Mg(2+) - ATP was found to be controlled by the same step at 25 degrees C. In all three cases, this rate-limiting step is changed in the same way by lowereing temperature. 3. Using the chemically determined molecular weights for myosin light chains, their stoichiometry was found on the basis of sodium dodecyl sulfate electrophoresis to be 1.2 : 2.1 : 0.8 for light chain-1: light chain-2:light chain-3 per molecule of fast myosin, 2.0 : 1.9 for light chain-1:light chain-2 per molecule of slow myosin and 1.9 : 1.9 for light chain-1:light chain-2 per molecule of cardiac myosin. This qualitative difference in light subunit composition between the fast and the two types of slow myosin is not reflected in the small variations of the characteristics exhibited by the isolated myosins, but rather seems to be connected with their respective myofibrillar ATPase activities." }, "ArticleTitle": "Radioactive labeling and location of specific thiol groups in myosin from fast, slow and cardiac muscles.", "AuthorList": { "Author": { "LastName": [ "Pfister", "Schaub", "Watterson", "Knecht", "Waser" ], "ForeName": [ "M", "M C", "J G", "M", "P G" ], "Initials": [ "M", "MC", "JG", "M", "PG" ], "CollectiveName": [ "", "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "SF19107" ], "Agency": [ "Biotechnology and Biological Sciences Research Council" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "Netherlands" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "EC 3.6.1.-", "EC 3.6.4.1", "I38ZP9992A", "O3C74ACM9V", "RWP5GA015D" ], "NameOfSubstance": [ "Sulfhydryl Compounds", "Adenosine Triphosphatases", "Myosins", "Magnesium", "Ethylmaleimide", "Potassium" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adenosine Triphosphatases", "Animals", "Binding Sites", "Enzyme Activation", "Ethylmaleimide", "Hydrogen-Ion Concentration", "Kinetics", "Magnesium", "Molecular Weight", "Muscle, Smooth", "Muscles", "Myocardium", "Myosins", "Potassium", "Protein Binding", "Protein Conformation", "Rabbits", "Sulfhydryl Compounds", "Swine", "Temperature" ], "QualifierName": [ "analysis", "", "", "drug effects", "pharmacology", "", "", "pharmacology", "", "enzymology", "enzymology", "enzymology", "analysis", "pharmacology", "", "", "", "analysis", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "73", "0005-2744(75)90220-X", "10.1016/0005-2744(75)90220-x" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 11, 11, 11 ], "Day": [ 20, 20, 20 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 104, "DateCompleted": { "Year": 1976, "Month": 2, "Day": 19 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2017, "Month": 9, "Day": 22 }, "Article": { "Abstract": { "AbstractText": "Experiments were conducted on male rats. A study was made of the content of nicotinamide coenzymes in the liver and myocardium 24 hours after the administration of 0.5 ml of dichloroethane into the stomach. In parallel with disturbance of the morphological structure of the liver and of the myocardium, increase in the activity of alanine and aspargic aminotranspherases in the blood serum, dichloroethane reduced the content of nicotinamide coenzymes and deranged the ratio of their oxidized and reduced forms in these organs." }, "ArticleTitle": "[Level of nicotinamide coenzymes in the liver and myocardium of rats poisoned with dichlorethane].", "AuthorList": { "Author": { "LastName": [ "Natsiuk", "Chekman" ], "ForeName": [ "M V", "I S" ], "Initials": [ "MV", "IS" ], "CollectiveName": [ "", "" ] } }, "Language": "rus", "GrantList": { "Grant": { "GrantID": [ "G0502121" ], "Agency": [ "Medical Research Council" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "English Abstract", "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "Russia (Federation)" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0U46U6E8UK", "53-59-8", "EC 2.6.1.1", "EC 2.6.1.2" ], "NameOfSubstance": [ "Ethylene Dichlorides", "Hydrocarbons, Chlorinated", "NAD", "NADP", "Aspartate Aminotransferases", "Alanine Transaminase" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Alanine Transaminase", "Animals", "Aspartate Aminotransferases", "Ethylene Dichlorides", "Heart", "Hydrocarbons, Chlorinated", "Liver", "Male", "Myocardium", "NAD", "NADP", "Rats" ], "QualifierName": [ "blood", "", "blood", "poisoning", "drug effects", "poisoning", "drug effects", "", "metabolism", "metabolism", "metabolism", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "104" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 4, 4, 4 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 129, "DateCompleted": { "Year": 1976, "Month": 2, "Day": 20 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 6, "Day": 13 }, "Article": { "Abstract": { "AbstractText": "(1) Crude synaptosomal fractions (P2) derived from guinea-pig cerebral cortex were incubated in the presence of 50 mM KCl in a Krebs-glucose medium. Torpedo marmorata electric organs were stimulated electrically in vivo at 5 pulses/sec for 30 min by electrodes placed on the electric lobe. Synaptic vesicles were isolated from each source and the phospholipid compositions analysed and compared with vesicles from unstimulated controls. (2) Lysophosphatidylcholine was the only lysophosphoglyceride demonstrable in the synaptic vesicles from either source and its low levels did not increase as a result of chemical or electircal stimulation. In each case there was a close similarity of the phospholipid distributions in the vesicles taken from control and stimulated samples. (3) Control experiments indicated extensive decreases in the acetylcholine content of the vesicles from the stimulated electric organ and smaller decreases in the acetylcholine content of the synaptic vesicles from stimulated crude synaptosomal fractions. These fractions were found to respire linearly in the presence of 10 mM glucose and the vesicle fractions were shown to have low levels of contaiminating membranes as judged by marker enzyme analyses. (4) Crude synaptosomal fractions from guinea-pig cerebral cortex were incubated in a Krebs-glucose medium with labelled fatty acids and [3H]glucose in the presence or absence of 50 mM KCl. Subsynaptosomal fractionation was carried out and specific radioactivities of phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine and phosphatidylinositol were determined in fractions D (synaptic vesicles), E (microsomes) and H (disrupted synaptosomes). The release of neurotransmitter did not significantly enhance the labelling of phospholipids in any of the fractions studied as compared with phospholipids from unstimulated fractions. This was found after two incubation times and using [14C]oleate, [14C]arachidonate, [3H]palmitate and [3H]glucose." }, "ArticleTitle": "The involvement of lysophosphoglycerides in neurotransmitter release; the composition and turnover of phospholipids of synaptic vesicles of guinea-pig cerebral cortex and Torpedo electric organ and the effect of stimulation.", "AuthorList": { "Author": { "LastName": [ "Baker", "Dowdall", "Whittaker" ], "ForeName": [ "R R", "M J", "V P" ], "Initials": [ "RR", "MJ", "VP" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "100406" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "Netherlands" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "0", "0", "EC 3.1.1.8", "N9YNS0M02X" ], "NameOfSubstance": [ "Neurotransmitter Agents", "Phosphatidylcholines", "Phosphatidylethanolamines", "Phosphatidylserines", "Phospholipids", "Cholinesterases", "Acetylcholine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Acetylcholine", "Animals", "Cerebral Cortex", "Cholinesterases", "Electric Organ", "Electric Stimulation", "Guinea Pigs", "Microsomes", "Neurotransmitter Agents", "Oxygen Consumption", "Phosphatidylcholines", "Phosphatidylethanolamines", "Phosphatidylserines", "Phospholipids", "Synaptic Vesicles", "Synaptosomes" ], "QualifierName": [ "metabolism", "", "metabolism", "metabolism", "metabolism", "", "", "metabolism", "metabolism", "", "metabolism", "metabolism", "metabolism", "metabolism", "enzymology", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "129", "0006-8993(75)90162-6", "10.1016/0006-8993(75)90162-6" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 12, 12, 12 ], "Day": [ 26, 26, 26 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 156, "DateCompleted": { "Year": 1976, "Month": 2, "Day": 26 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2020, "Month": 2, "Day": 25 }, "Article": { "Abstract": { "AbstractText": "The rate of coronary blood flow was varied in isolated working rat heart preparations to determine its influence on the rate of glocose utilization, tissue high-energy phosphates, and intracellular pH. A 60% reduction in coronary blood flow resulted in a 30% reduction in oxygen consumption, an accelerated rate of glusoe utilization, lower tissue levels of high-energy phosphate, and higher tissue levels of lactate and H+. Ventricular performance deteriorated as reflected by a decrease in heart rate and peak systolic pressure. Further reductions in coronary blood flow resulted in inhibition of glycolysis, a greater decrease in tissue levels of high-energy phosphates, and higher tissue levels of both lactate and H+. These changes in glycolytic flux, tissue metabolites, and ventricular performance were proportional to the degree of restriction in coronary blood flow. The importance of coronary blood flow and washout of the interstitial space in the maintenance of accelerated glycolytic flux in oxygen-deficient hearts is emphasized. It is concluded that acceleration of ATP production from glycolysis can occur only in the marginally ischemic tissue in the peripheral area of tissue supplied by an occluded artery. The central area of tissue which receives a low rate of coronary blood flow will have a reduced rate of ATP production due to both a lack of oxygen and an inhibition of glycolysis." }, "ArticleTitle": "Effect of coronary blood flow on glycolytic flux and intracellular pH in isolated rat hearts.", "AuthorList": { "Author": { "LastName": [ "Neely", "Whitmer", "Rovetto" ], "ForeName": [ "J R", "J T", "M J" ], "Initials": [ "JR", "JT", "MJ" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "G1001344" ], "Agency": [ "Medical Research Council" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "020IUV4N33", "8L70Q75FXE" ], "NameOfSubstance": [ "Lactates", "Phosphocreatine", "Adenosine Triphosphate" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adenosine Triphosphate", "Animals", "Blood Flow Velocity", "Coronary Circulation", "Glycolysis", "Heart", "Hydrogen-Ion Concentration", "In Vitro Techniques", "Lactates", "Male", "Myocardium", "Oxygen Consumption", "Phosphocreatine", "Rats" ], "QualifierName": [ "analysis", "", "", "", "", "physiology", "", "", "analysis", "", "analysis", "", "analysis", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "156", "10.1161/01.res.37.6.733" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 12, 12, 12 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 171, "DateCompleted": { "Year": 1976, "Month": 2, "Day": 19 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 10, "Day": 21 }, "Article": { "Abstract": { "AbstractText": "1. We measured the minute ventilation and arterial blood catecholamine concentrations in four normal men standing and at two levels of moderate treadmill exercise breathing 14% oxygen or air. 2. Minute ventilation was significantly higher during hypoxic exercise than during normoxic exercise at an oxygen uptake of 1500 ml/min. 3. Arterial plasma noradrenaline during hypoxic exercise at an oxygen uptake of 1500 ml/min was significantly greater than at rest. 4. Arterial plasma noradrenaline during normoxic exercise at an oxygen uptake of 1500 ml/min was not elevated above the resting concentration. 5. The results are compatible with the suggestion that increased concentrations of arterial plasma noradrenaline contribute to the hypoxic potentiation of the respiratory response to moderate exercise." }, "ArticleTitle": "Arterial catecholamines in hypoxic exercise in man.", "AuthorList": { "Author": { "LastName": [ "Clancy", "Critchley", "Leitch", "Kirby", "Ungar", "Flenley" ], "ForeName": [ "L J", "J A", "A G", "B J", "A", "D C" ], "Initials": [ "LJ", "JA", "AG", "BJ", "A", "DC" ], "CollectiveName": [ "", "", "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "G0501542" ], "Agency": [ "Medical Research Council" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "S88TT14065", "X4W3ENH1CV", "YKH834O4BH" ], "NameOfSubstance": [ "Oxygen", "Norepinephrine", "Epinephrine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adult", "Arteries", "Epinephrine", "Humans", "Hydrogen-Ion Concentration", "Hypoxia", "Male", "Norepinephrine", "Oxygen", "Physical Exertion", "Respiration" ], "QualifierName": [ "", "", "blood", "", "", "blood", "", "blood", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "171", "10.1042/cs0490503" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 11, 11, 11 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 251, "DateCompleted": { "Year": 1976, "Month": 2, "Day": 21 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2018, "Month": 4, "Day": 29 }, "Article": { "Abstract": { "AbstractText": "Some derivatives of isoindoline were prepared in order to test their cardiovascular activity. Pharmacological tests showed that some of the compounds had moderate alpha-blocking and coronarodilatory activity whereas others had some local anesthetic activity." }, "ArticleTitle": "[Synthesis of N-substituted isoindolines].", "AuthorList": { "Author": { "LastName": [ "Chimenti", "Vomero" ], "ForeName": [ "F", "S" ], "Initials": [ "F", "S" ], "CollectiveName": [ "", "" ] } }, "Language": "ita", "GrantList": { "Grant": { "GrantID": [ "101784" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "English Abstract", "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "Italy" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "0", "0" ], "NameOfSubstance": [ "Adrenergic beta-Antagonists", "Anesthetics, Local", "Benzimidazoles", "Indoles", "Vasodilator Agents" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adrenergic beta-Antagonists", "Anesthetics, Local", "Benzimidazoles", "Indoles", "Vasodilator Agents" ], "QualifierName": [ "chemical synthesis", "chemical synthesis", "", "chemical synthesis", "chemical synthesis" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "251" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 11, 11, 11 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 376, "DateCompleted": { "Year": 1976, "Month": 2, "Day": 21 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2020, "Month": 2, "Day": 25 }, "Article": { "Abstract": { "AbstractText": "In order to clarify how the electrophoretic behavior reflects the conformational transition of globular proteins, moving boundary electrophoresis was applied to analysis of the acid conformational change of alpha-lactalbumin. The appearance of only a single electrophoretic boundary in the transition region of the protein suggests a very rapid transition with a half-time estimated to be smaller than 7 min on the basis of the theory of isomerizing systems in electrophoresis. The transition is clearly reflected in the dependence of the mobility on the protein net charge, which shows a sigmoidal curve closely similar to that obtained by a Linderstrøm-Lang pH-tritration plot for the carboxyl groups of alpha-lactalbumin. It was also concluded from the transition curves that the acidfication does not result in complete unfolding, but that a compact structure is maintained in the acidic region with an apparently expanded form as compared to the native state of the protein. All results obtained by electrophoresis were also supported by the results of pH-jump studies, analytical gel chromatography, and CD measurements." }, "ArticleTitle": "Electrophoretic investigations of the acid conformational change of alpha-lactalbumin.", "AuthorList": { "Author": { "LastName": [ "Kuwajima", "Nitta", "Sugai" ], "ForeName": [ "K", "K", "S" ], "Initials": [ "K", "K", "S" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "090441" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "9013-90-5" ], "NameOfSubstance": [ "Myoglobin", "Lactalbumin" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Circular Dichroism", "Electrophoresis", "Hydrogen-Ion Concentration", "Lactalbumin", "Myoglobin", "Protein Conformation", "Time Factors" ], "QualifierName": [ "", "", "", "", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "376" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 7, 7, 7 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 385, "DateCompleted": { "Year": 1976, "Month": 2, "Day": 9 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2021, "Month": 2, "Day": 10 }, "Article": { "Abstract": { "AbstractText": "Reduced coenzyme Q-cytochrome c reductase from bovine heart mitochondria (complex III) was incorporated into phospholipid vesicles by the cholate dialysis procedure. Soybean phospholipids or mixtures of purified phosphatidylcholine, phosphatidylethanolamine, and cardiolipin could be used. Oxidation of reduced coenzyme Q2 by the reconstituted vesicles with cytochrome c as oxidant showed the following energy-coupling phenomena. 1. Protons were translocated outward with a coupling ratio, H+/2e, of 1.9 +/- 0.2. Measurements with mitochondria under similar conditions showed an H+/2e ratio of 1.8. Proton translocation was not seen in the presence of uncoupling agents and was in addition to the net acidification of the medium from the over-all oxidation reaction. 2. Potassium ions were taken up by the reconstituted vesicles in the presence of valinomycin in a reaction coupled to electron transfer. The coupling ratio for K+ uptake, K+/2e, was 2.0 in the vesicles and approximately 1.5 in mitochondria. 3. The rate of oxidation of reduced coenzyme Q2 by the reconstituted vesicles was stimulated up to 10-fold by uncouplers or by valinomycin plus nigericin and K+ ions. Addition of valinomycin alone in a K+ medium caused a transient stimulation of electron transfer. The results indicate that energy coupling can be observed with isolated reduced coenzyme Q-cytochrome c reductase if the enzyme complex is properly incorporated into a phospholipid vesicle." }, "ArticleTitle": "Reconstitution of ion transport and respiratory control in vesicles formed from reduced coenzyme Q-cytochrome c reductase and phospholipids.", "AuthorList": { "Author": { "LastName": [ "Leung", "Hinkle" ], "ForeName": [ "K H", "P C" ], "Initials": [ "KH", "PC" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "090441" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "1339-63-5", "EC 1.6.2.-", "RWP5GA015D" ], "NameOfSubstance": [ "Cholic Acids", "Ionophores", "Phospholipids", "Ubiquinone", "Cytochrome Reductases", "Potassium" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Animals", "Biological Transport, Active", "Cattle", "Cholic Acids", "Cytochrome Reductases", "Electron Transport", "Hydrogen-Ion Concentration", "Ionophores", "Kinetics", "Mitochondria, Muscle", "Models, Biological", "Myocardium", "Oxygen Consumption", "Phospholipids", "Potassium", "Ubiquinone" ], "QualifierName": [ "", "", "", "pharmacology", "metabolism", "", "", "pharmacology", "", "drug effects", "", "", "drug effects", "pharmacology", "metabolism", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "385", "S0021-9258(19)40782-5" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 11, 11, 11 ], "Day": [ 10, 10, 10 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 609, "DateCompleted": { "Year": 1976, "Month": 2, "Day": 26 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 8, "Day": 18 }, "Article": { "Abstract": { "AbstractText": "Experiments were carried out to define the kinetic parameters of the major phosphate transport processes of rat liver mitochondria, and to obtain information about the molecular properties of these systems." }, "ArticleTitle": "Phosphate transport in rat liver mitochondria. Kinetics, inhibitor sensitivity, energy requirements, and labeled components.", "AuthorList": { "Author": { "LastName": [ "Coty", "Pedersen" ], "ForeName": [ "W A", "P L" ], "Initials": [ "WA", "PL" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "100406" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, Non-P.H.S.", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "Netherlands" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "0", "0", "0", "0", "03L9OT429T", "57-50-1", "O3C74ACM9V", "RRU6GY95IS" ], "NameOfSubstance": [ "Dinitrophenols", "Malates", "Malonates", "Mercuribenzoates", "Oligomycins", "Oxazoles", "Phosphates", "Rotenone", "Sucrose", "Ethylmaleimide", "Nigericin" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Animals", "Biological Transport, Active", "Dinitrophenols", "Ethylmaleimide", "Hydrogen-Ion Concentration", "Kinetics", "Malates", "Male", "Malonates", "Membranes", "Mercuribenzoates", "Mitochondria, Liver", "Mitochondrial Swelling", "Nigericin", "Oligomycins", "Oxazoles", "Phosphates", "Rats", "Rotenone", "Sucrose" ], "QualifierName": [ "", "", "pharmacology", "pharmacology", "", "", "metabolism", "", "pharmacology", "metabolism", "pharmacology", "drug effects", "", "pharmacology", "pharmacology", "metabolism", "metabolism", "", "pharmacology", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "609", "10.1007/BF01732202" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 11, 11, 11 ], "Day": [ 14, 14, 14 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 1002, "DateCompleted": { "Year": 1976, "Month": 2, "Day": 21 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 5, "Day": 1 }, "Article": { "Abstract": { "AbstractText": "Peptic and chymotryptic peptides were isolated form the NADP-specific glutamate dehydrogenase of Neurospora crassa and substantially sequenced. Out of 452 residues in the polypeptide chain, 265 were recovered in the peptic and 427 in the chymotryptic peptides. Together with the tryptic peptides [Wootton, J. C., Taylor, J. G., Jackson, A. A., Chambers, G. K. & Fincham, J. R. S. (1975) Biochem. J. 149, 749-755], these establish the complete sequence of the chain, including the acid and amide assignments, except for seven places where overlaps are inadequate. These remaining alignments are deduced from information on the CNBr fragments obtained in another laboratory [Blumenthal, K. M., Moon, K. & Smith, E. L. (1975), J. Biol. Chem. 250, 3644-3654]. Further information has been deposited as Supplementary Publication SUP 50054 (17 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained under the terms given in Biochem. J. (1975) 145, 5." }, "ArticleTitle": "The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptic and chymotryptic peptides and the complete sequence.", "AuthorList": { "Author": { "LastName": [ "Holder", "Wootton", "Baron", "Chambers", "Fincham" ], "ForeName": [ "A A", "J C", "A J", "G K", "J R" ], "Initials": [ "AA", "JC", "AJ", "GK", "JR" ], "CollectiveName": [ "", "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "G1000191" ], "Agency": [ "Medical Research Council" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "53-59-8", "EC 1.4.1.2", "EC 3.4.21.1", "EC 3.4.23.1" ], "NameOfSubstance": [ "Amides", "Amino Acids", "Peptide Fragments", "NADP", "Glutamate Dehydrogenase", "Chymotrypsin", "Pepsin A" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Amides", "Amino Acid Sequence", "Amino Acids", "Chymotrypsin", "Glutamate Dehydrogenase", "NADP", "Neurospora", "Neurospora crassa", "Pepsin A", "Peptide Fragments" ], "QualifierName": [ "analysis", "", "analysis", "", "analysis", "", "enzymology", "enzymology", "", "analysis" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "1002", "PMC1165685", "10.1042/bj1490757" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 9, 9, 9 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 1081, "DateCompleted": { "Year": 1976, "Month": 3, "Day": 20 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 7, "Day": 4 }, "Article": { "Abstract": { "AbstractText": "Four distinct peptide hydrolases (EC 3-4) have been characterized in guinea-pig epidermis; these are cathepsin B1, cathepsin C, cathepsin D and arylamidase. Their properties are consistent with those of lysosomal enzymes. Cathepsin E was not detected." }, "ArticleTitle": "Lysosomal hydrolases of the epidermis. 3. Peptide hydrolases.", "AuthorList": { "Author": { "LastName": [ "Mier", "van den Hurk" ], "ForeName": [ "P D", "J J" ], "Initials": [ "PD", "JJ" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "100591" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "5UX2SD1KE2", "EC 3.4.-", "EC 3.4.-", "EC 3.4.11.-", "K848JZ4886" ], "NameOfSubstance": [ "Chlorides", "Cysteamine", "Cathepsins", "Peptide Hydrolases", "Aminopeptidases", "Cysteine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Aminopeptidases", "Animals", "Cathepsins", "Chlorides", "Cysteamine", "Cysteine", "Enzyme Activation", "Guinea Pigs", "Hydrogen-Ion Concentration", "Kinetics", "Lysosomes", "Peptide Hydrolases", "Skin" ], "QualifierName": [ "analysis", "", "analysis", "", "", "", "", "", "", "", "enzymology", "metabolism", "enzymology" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "1081", "10.1111/j.1365-2133.1975.tb02243.x" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 11, 11, 11 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 2009, "DateCompleted": { "Year": 1976, "Month": 3, "Day": 20 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2021, "Month": 12, "Day": 3 }, "Article": { "Abstract": { "AbstractText": "The mean PNK activity in red blood cells from black subjects was only about 40% of that in whites. Among 51 whites examined, one was found to have enzyme deficiency. The estimated gene frequencies for PNKH (the common allele in whites which codes for higher enzyme activity) and PNKL (the common allele in blacks which codes for lower enzyme activity) were .35 and .65, respectively, for black donors, and .81 and .19, respectively, for white donors, The variant enzyme in persons with enzyme deficiency was associated with an increased rate of degradation in red cells during aging. No other biochemical or electrophoretic differences were detected." }, "ArticleTitle": "Biochemical and electrophoretic studies of erythrocyte pyridoxine kinase in white and black Americans.", "AuthorList": { "Author": { "LastName": [ "Chern", "Beutler" ], "ForeName": [ "C J", "E" ], "Initials": [ "CJ", "E" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "090441" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Comparative Study", "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "EC 2.7.-", "EC 2.7.1.1" ], "NameOfSubstance": [ "Phosphotransferases", "Hexokinase" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Alleles", "Blacks", "Erythrocytes", "Gene Frequency", "Genes", "Hexokinase", "Humans", "Hydrogen-Ion Concentration", "Pedigree", "Phenotype", "Phosphotransferases", "Temperature", "United States", "Whites" ], "QualifierName": [ "", "", "enzymology", "", "", "metabolism", "", "", "", "", "blood", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "2009", "PMC1684914" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1976, 1976, 1976 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 2010, "DateCompleted": { "Year": 1976, "Month": 4, "Day": 2 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2017, "Month": 9, "Day": 22 }, "Article": { "Abstract": { "AbstractText": "This project involved designing, developing and evaluating a simulation module, utilizing the latent image technique. The general topic chosen for this simulation was the laboratory characterization of anemias. Target learner populations included medical technology students, physician assistant students, and pathology residents. Members of all three groups participated in the evaluation of the module and responded to its use in varied settings." }, "ArticleTitle": "Use of the latent image technique to develop and evaluate problem-solving skills.", "AuthorList": { "Author": { "LastName": [ "Schwabbauer" ], "ForeName": [ "M L" ], "Initials": [ "ML" ], "CollectiveName": [ "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "MC_UU_12020/7" ], "Agency": [ "Medical Research Council" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [], "NameOfSubstance": [] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Anemia", "Hematuria", "Humans", "Iowa", "Medical Laboratory Science", "Models, Psychological", "Physician Assistants", "Problem Solving", "Teaching", "Teaching Materials" ], "QualifierName": [ "diagnosis", "complications", "", "", "education", "", "education", "", "methods", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "2010" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 12, 12, 12 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 2011, "DateCompleted": { "Year": 1976, "Month": 3, "Day": 15 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2021, "Month": 1, "Day": 7 }, "Article": { "Abstract": { "AbstractText": "A review of drug treatment for Down's syndrome individuals was presented. Drugs used to modify behavior, as well as drugs used with the goal of affecting cognitive processes, were discussed. Some observations were offered as to the effectiveness of past and current drugs on Down's syndrome and some methodological problems relating to drug studies presented. There have not been any drugs that have demonstrated remarkable improvement in the status of Down's syndrome individuals that have been widely accepted as effective." }, "ArticleTitle": "Review of drug treatment for Down's syndrome persons.", "AuthorList": { "Author": { "LastName": [ "Share" ], "ForeName": [ "J B" ], "Initials": [ "JB" ], "CollectiveName": [ "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "HERU1" ], "Agency": [ "Chief Scientist Office" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "0", "0", "0", "0", "0", "0", "333DO1RDJY", "C1LJO185Q9" ], "NameOfSubstance": [ "Amphetamines", "Antipsychotic Agents", "Glutamates", "Minerals", "Phenothiazines", "Pituitary Hormones", "Psychotropic Drugs", "Thyroid Hormones", "Vitamins", "Serotonin", "5-Hydroxytryptophan" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "5-Hydroxytryptophan", "Amphetamines", "Antipsychotic Agents", "Behavior", "Cell Transplantation", "Cognition", "Down Syndrome", "Drug Evaluation", "Enzyme Therapy", "Glutamates", "Humans", "Minerals", "Phenothiazines", "Pituitary Hormones", "Psychotropic Drugs", "Research Design", "Serotonin", "Thyroid Hormones", "Vitamins" ], "QualifierName": [ "therapeutic use", "therapeutic use", "therapeutic use", "drug effects", "", "drug effects", "drug therapy", "", "", "therapeutic use", "", "therapeutic use", "", "therapeutic use", "therapeutic use", "", "therapeutic use", "therapeutic use", "therapeutic use" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "2011" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1976, 1976, 1976 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 2012, "DateCompleted": { "Year": 1976, "Month": 3, "Day": 15 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 6, "Day": 15 }, "Article": { "Abstract": { "AbstractText": "Using a combined special glass electrode it is possible to monitor pH ratios and pH variation in the subcutaneous tissue of the infant scalp continuously. Tests on a normal sample of newborn babies immediately after birth showed a significant correlation between tissue pH and capillary blood pH, with the trend of pH variation being broadly similar in both measurement media." }, "ArticleTitle": "Development of a special electrode for continuous subcutaneous pH measurement in the infant scalp.", "AuthorList": { "Author": { "LastName": [ "Stamm", "Latscha", "Janecek", "Campana" ], "ForeName": [ "O", "U", "P", "A" ], "Initials": [ "O", "U", "P", "A" ], "CollectiveName": [ "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "090441" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [], "NameOfSubstance": [] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Electrodes", "Fetal Blood", "Glass", "Humans", "Hydrogen-Ion Concentration", "Infant, Newborn", "Monitoring, Physiologic", "Scalp" ], "QualifierName": [ "", "", "", "", "", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "2012", "S0002-9378(16)33297-5", "10.1016/s0002-9378(16)33297-5" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1976, 1976, 1976 ], "Month": [ 1, 1, 1 ], "Day": [ 15, 15, 15 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 2013, "DateCompleted": { "Year": 1976, "Month": 3, "Day": 30 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 6, "Day": 15 }, "Article": { "Abstract": { "AbstractText": "We conducted a controlled, prospective trial to evaluate the effectiveness of rapidly infusing sodium bicarbonate (NaHCO3) and salt-poor albumin into high-risk, premature infants in the first 2 hours of life. Fifty-three infants, randomized into one of four treatment groups, received 8 ml. per kilogram of a solution containing either (A) glucose in water, (B) salt-poor albumin, (C) NaHCO3, or (D) a combination of albumin and NaHCO3. After the initial infusion, the babies received no colloid or alkali solutions until 4 hours of age. We managed them supportively with warmth, appropriate oxygen administration, isotonic fluid infusion, and close monitoring. Among the infants who received alkali, 14 of 26 acquired the respiratory distress syndrome (RDS), 11 died, and four had intracranial hemorrhage. Among babies who received no alkali, RDS occurred in 11 of 27, 5 died, and none had intracranial hemorrhage. These results do not support the common practice of rapidly infusing NaHCO3 into high-risk, premature infants, and they suggest that the early management of such infants needs renewed critical evaluation." }, "ArticleTitle": "Rapid infusion of sodium bicarbonate and albumin into high-risk premature infants soon after birth: a controlled, prospective trial.", "AuthorList": { "Author": { "LastName": [ "Bland", "Clarke", "Harden" ], "ForeName": [ "R D", "T L", "L B" ], "Initials": [ "RD", "TL", "LB" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "095121", "083942", "095938", "089752", "098497" ], "Agency": [ "Wellcome Trust", "Wellcome Trust", "Wellcome Trust", "Wellcome Trust", "Wellcome Trust" ], "Country": [ "United Kingdom", "United Kingdom", "United Kingdom", "United Kingdom", "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Clinical Trial", "Journal Article", "Randomized Controlled Trial" ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "142M471B3J", "9NEZ333N27" ], "NameOfSubstance": [ "Albumins", "Bicarbonates", "Carbon Dioxide", "Sodium" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Acidosis", "Albumins", "Bicarbonates", "Carbon Dioxide", "Cerebral Hemorrhage", "Female", "Hawaii", "Humans", "Hydrogen-Ion Concentration", "Infant, Newborn", "Infant, Premature, Diseases", "Infusions, Parenteral", "Male", "Prospective Studies", "Respiratory Distress Syndrome, Newborn", "Sodium", "Time Factors" ], "QualifierName": [ "drug therapy", "administration & dosage", "administration & dosage", "blood", "mortality", "", "", "", "", "", "blood", "", "", "", "mortality", "administration & dosage", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "2013", "0002-9378(76)90154-X", "10.1016/0002-9378(76)90154-x" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1976, 1976, 1976 ], "Month": [ 2, 2, 2 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 2014, "DateCompleted": { "Year": 1976, "Month": 3, "Day": 11 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2018, "Month": 4, "Day": 29 }, "Article": { "Abstract": { "AbstractText": "The effects of pH variation on ionic exchange and mechanical function were studied in the arterially perfused rat and rabbit septa. The pH and PCO2 of the control perfusate were 7.40 and 39 mmHg, respectively. In the rabbit septum a metabolic acidosis (pH equals 6.82, PCO2 equals 39 mmHg) caused a loss of 16% of control tension in 12 min. Na+ and K+ exchange were unaltered. A comparable respiratory acidosis (pH equals 6.81, PCO2 equals 159 mmHg) caused a 51% loss of tension in 2 min. Na+ exchange was unaltered but K+ efflux fell from 8.9 +/- 0.6 (mean +/- SE) to 4.9 +/- 0.3 mmol/kg dry wt per min (P less than 0.001, n equals 10). A net gain of K+ of 16.9 +/- 1.7 (n equals 14) mmol/kg dry wt occurred and was attributable to a delayed fall in K+ influx relative to efflux over 15 min. The net gain could not be mimicked by epinephrine administration or blocked by propranolol and was absent in the beating rat septum and the quiescent rabbit septum. These results suggest that the net uptake of K+, which appears to be dependent on a period of depolarization, and the changes of contractility are controlled by the H+ ion concentration at a cellular site whose exchange with the extracellular space is characterized by a considerable restriction of diffusion. Changes of contractility are not related to the net uptake of K+." }, "ArticleTitle": "Effect of pH on ionic exchange and function in rat and rabbit myocardium.", "AuthorList": { "Author": { "LastName": [ "Poole-Wilson", "Langer" ], "ForeName": [ "P A", "G A" ], "Initials": [ "PA", "GA" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "091038", "100591", "095938", "100544", "090441", "097903", "097170", "100406", "100921", "095495", "084655", "101234" ], "Agency": [ "Wellcome Trust", "Wellcome Trust", "Wellcome Trust", "Wellcome Trust", "Wellcome Trust", "Wellcome Trust", "Wellcome Trust", "Wellcome Trust", "Wellcome Trust", "Wellcome Trust", "Wellcome Trust", "Wellcome Trust" ], "Country": [ "United Kingdom", "United Kingdom", "United Kingdom", "United Kingdom", "United Kingdom", "United Kingdom", "United Kingdom", "United Kingdom", "United Kingdom", "United Kingdom", "United Kingdom", "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "9NEZ333N27", "9Y8NXQ24VQ", "RWP5GA015D", "YKH834O4BH" ], "NameOfSubstance": [ "Sodium", "Propranolol", "Potassium", "Epinephrine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Acidosis", "Acidosis, Respiratory", "Alkalosis, Respiratory", "Animals", "Epinephrine", "Heart", "Hydrogen-Ion Concentration", "In Vitro Techniques", "Ion Exchange", "Male", "Myocardium", "Perfusion", "Potassium", "Propranolol", "Rabbits", "Rats", "Sodium" ], "QualifierName": [ "chemically induced", "chemically induced", "chemically induced", "", "pharmacology", "drug effects", "", "", "", "", "metabolism", "", "metabolism", "pharmacology", "", "", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "2014", "10.1152/ajplegacy.1975.229.3.570" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 9, 9, 9 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 2015, "DateCompleted": { "Year": 1976, "Month": 3, "Day": 11 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2018, "Month": 4, "Day": 29 }, "Article": { "Abstract": { "AbstractText": "It has been established that H+ secretion can be maintained in frog stomach in the absence of exogenous CO2 by using a nutrient bathing fluid containing 25 mM H2PO4 (pH approximately equal to 4.5) or by lowering the pH of a nonbuffered nutrient solution to about 3.0-3.6. Exogenous CO2 in the presence of these nutrient solutions uniformly caused a marked decrease in H+ secretion, PD, adn short-circuit current (Isc) and an increase in transmucosal resistance (R). Elevation of nutrient [k+] to 83 mM reduced R significantly but transiently without change in H+ when nutrient pH less than 5.0, whereas R returned to base line and H+ increased when nutrient pH greater than 5.0. Acidification of the nutrient medium in the presence of exogenous CO2 results in inhibition of the secretory pump, probably by decreasing intracellular pH, and also interferes with conductance at the nutrient membrane. Removal of exogenous CO2 from standard bicarbonate nutrient solution reduced by 50% the H+, PD, and Isc without change in R; K+-free nutrient solutions reverse these changes in Isc and PD but not in H+. The dropping PD and rising R induced by K+-free nutrient solutions in 5% CO2 - 95% O2 are returned toward normal by 100% O2. Our findings support an important role for exogenous CO2 in maintaining normal acid-base balance in frog mucosa by acting as an acidifying agent." }, "ArticleTitle": "Acid-base balance in amphibian gastric mucosa.", "AuthorList": { "Author": { "LastName": [ "Silen", "Machen", "Forte" ], "ForeName": [ "W", "T E", "J G" ], "Initials": [ "W", "TE", "JG" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "090532" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "142M471B3J", "RWP5GA015D" ], "NameOfSubstance": [ "Bicarbonates", "Phosphates", "Solutions", "Carbon Dioxide", "Potassium" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Acid-Base Equilibrium", "Animals", "Anura", "Bicarbonates", "Carbon Dioxide", "Electrophysiology", "Gastric Mucosa", "Hydrogen-Ion Concentration", "Phosphates", "Potassium", "Rana catesbeiana", "Solutions" ], "QualifierName": [ "drug effects", "", "", "pharmacology", "pharmacology", "", "drug effects", "", "pharmacology", "pharmacology", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "2015", "10.1152/ajplegacy.1975.229.3.721" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 9, 9, 9 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 2286, "DateCompleted": { "Year": 1976, "Month": 4, "Day": 29 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 6, "Day": 12 }, "Article": { "Abstract": { "AbstractText": "A method of isolation of alpha-1-antitrypsin (alpha-1-AT) in good yield from normal human plasma is described. A key step was affinity chromatography employing an antiserum which had been depleted of alpha-1-AT antibodies. The final preparations were homogeneous by immunological and physicochemical criteria. The specific activity of the purified alpha-1-AT was 0.363 mg of active bovine trypsin inhibited per 1.0 mg of inhibitor. Polyacrylamide gel patterns at both alkaline and acid pH of highly pure preparations frequently, but not invariably, showed multiple hands. Molecular weight studies by sedimentation equilibrium ultracentrifugation in aqueous buffer and in 6 M guanidine as well as sodium dodecyl sulfate polyacrylamide gel electrophoresis suggest that alpha-1-AT is a single polypeptide chain having a molecular weight of 49,500. Other physical and chemical properties of the inhibitor are described. A limited N-terminal sequence (Glu-Asp-Pro-Gln-Gly-Asx-Ala-Ala) was obtained. It was found that alpha-1-AT easily forms polymers and higher aggregates when exposed to denaturing agents such as 8 M urea and 6 M guanidine. The results suggest that aggregation is determined by both covalent and noncovalent forces." }, "ArticleTitle": "Isolation, chemical, and physical properties of alpha-1-antitrypsin.", "AuthorList": { "Author": { "LastName": [ "Musiani", "Tomasi" ], "ForeName": [ "P", "T B" ], "Initials": [ "P", "TB" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "R01 HD017013" ], "Agency": [ "NICHD NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0" ], "NameOfSubstance": [ "Amino Acids", "Hexoses", "alpha 1-Antitrypsin" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Amino Acid Sequence", "Amino Acids", "Chromatography, Affinity", "Electrophoresis, Polyacrylamide Gel", "Hexoses", "Humans", "Hydrogen-Ion Concentration", "Molecular Weight", "Protein Denaturation", "Spectrophotometry, Ultraviolet", "alpha 1-Antitrypsin" ], "QualifierName": [ "", "analysis", "", "", "analysis", "", "", "", "", "", "isolation & purification" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "2286", "10.1021/bi00649a011" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1976, 2001, 1976 ], "Month": [ 2, 3, 2 ], "Day": [ 24, 28, 24 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 2329, "DateCompleted": { "Year": 1976, "Month": 4, "Day": 23 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2020, "Month": 12, "Day": 9 }, "Article": { "Abstract": { "AbstractText": "Highly purified L-asparaginase having a specific activity of 500+/- +/-40 IU./mg protein is isolated from Pseudomonas fluorescens AG cells. The purification procedure includes isopropanol fractionation, gel filtration through Sephadex G-100, chromatography on hydroxylapatite and DEAE-cellulose columns. The asparaginase preparation is homogenous on the basis of polyacrylamide gel electrophoresis data. The pH optimum is found to be 8.0-9.0, isoelectric point and molecular weight are 4.5+/-0.05 and 70,000+/-5,000 respectively, Km for L-asparagine being-4.1-10(-4)M. The enzyme does not hydrolyse L-glutamine. The hydrolysis rate of D-glutamine is less than 1% of the deamydation rate of L-isomer. p-Chloro-mercurium benzoate at a concentration of 10(-4) M completely inhibits the asparaginase activity. Asparaginase from Ps. fluorescens AG possesses and antileucosic activity, inhibiting 3H-thymidine incorporation into DNA of Berkit lymphoma cells." }, "ArticleTitle": "[Isolation and properties of a homogeneous L-asparaginase preparation from Pseudomonas fluorescens AG].", "AuthorList": { "Author": { "LastName": [ "Nilolaev", "Sokolov", "Kozlov", "Kutsman" ], "ForeName": [ "A Ia", "N N", "E A", "M E" ], "Initials": [ "AIa", "NN", "EA", "ME" ], "CollectiveName": [ "", "", "", "" ] } }, "Language": "rus", "GrantList": { "Grant": { "GrantID": [ "G0900274" ], "Agency": [ "Medical Research Council" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "Russia (Federation)" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0RH81L854J", "EC 3.5.1.1" ], "NameOfSubstance": [ "Chloromercuribenzoates", "DNA, Neoplasm", "Glutamine", "Asparaginase" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Asparaginase", "Burkitt Lymphoma", "Chloromercuribenzoates", "DNA, Neoplasm", "Glutamine", "Hydrogen-Ion Concentration", "Isoelectric Point", "Molecular Weight", "Pseudomonas fluorescens" ], "QualifierName": [ "antagonists & inhibitors", "metabolism", "pharmacology", "biosynthesis", "metabolism", "", "", "", "enzymology" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "2329" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 9, 9, 9 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 5451, "DateCompleted": { "Year": 1976, "Month": 8, "Day": 3 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2021, "Month": 2, "Day": 10 }, "Article": { "Abstract": { "AbstractText": "A method for assessing the binding of 3H-labeled prostaglandin E1 ([3H]PGE1) to cell membranes has been developed and used to study the interaction of [3H]PGE1 with membranes from cultured mammalian cells. Receptor sites were identified by correlation of the potency of a series of compounds to compete for [3H]PGE1 binding sites and to stimulate adenylate cyclase activity, by correlation of rates of binding and change in enzyme activity, and by the correspondence of [3H]PGE1-binding activity with the presence or absence of PGE1-sensitive adenylate cyclase in several clones. In clone B82, a murine L-cell, [3H]PGE1 binds with an activation energy of 14 kcal/mol to a class of sites with an affinity of 0.5 X 10(8) M-1 and a capacity of 150 fmol/mg of protein. Concentration dependence of adenylate cyclase activation by PGE1 (KD =30 nM) and kinetic analysis of [3H]PGE1 binding (k1 = 4 X 10(6) liters/mol/min, k-1 0.15/min) verify this affinity. Concentration dependence and specificity of binding and activation of adenylate cyclases in neuroblastoma clone N4TG1 and N18TG2 substantiate the method. In several clones that lack PGE1-responsive adenylate cyclase, no specific [3H]PGE1 binding is detectable." }, "ArticleTitle": "Binding of (3H)prostaglandin E1 to putative receptors linked to adenylate cyclase of cultured cell clones.", "AuthorList": { "Author": { "LastName": [ "Brunton", "Wiklund", "Van Arsdale", "Gilman" ], "ForeName": [ "L L", "R A", "P M", "A G" ], "Initials": [ "LL", "RA", "PM", "AG" ], "CollectiveName": [ "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "AM 17042", "GM 02139", "NS 10193" ], "Agency": [ "NIADDK NIH HHS", "NIGMS NIH HHS", "NINDS NIH HHS" ], "Country": [ "United States", "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "10028-17-8", "EC 4.6.1.1" ], "NameOfSubstance": [ "Prostaglandins", "Prostaglandins E", "Receptors, Cell Surface", "Tritium", "Adenylyl Cyclases" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adenylyl Cyclases", "Animals", "Binding Sites", "Cell Line", "Cell Membrane", "Dose-Response Relationship, Drug", "Hydrogen-Ion Concentration", "Kinetics", "L Cells", "Mice", "Neuroblastoma", "Prostaglandins", "Prostaglandins E", "Protein Binding", "Receptors, Cell Surface", "Temperature", "Tritium" ], "QualifierName": [ "metabolism", "", "", "", "enzymology", "", "", "", "metabolism", "", "metabolism", "pharmacology", "metabolism", "", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "5451", "S0021-9258(17)33496-8" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1976, 1976, 1976 ], "Month": [ 5, 5, 5 ], "Day": [ 25, 25, 25 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 7633, "DateCompleted": { "Year": 1976, "Month": 9, "Day": 25 }, "NumberOfReferences": 9, "DateRevised": { "Year": 2017, "Month": 9, "Day": 22 }, "Article": { "Abstract": { "AbstractText": "Urticaria is a problem often as vexing to the physician as to the patient. The approach to the patient with hives first demands a search for the etiology, whether endogenous and triggered by emotions or occult systemic disease, exogenous and triggered by allergy to inhaled or ingested antigens, or physical and due to abnormal sensitivity to heat, cold, light, or pressure. Often a fruitless search, the diagnostic evaluation must be accompanied by appropriate symptomatic therapy requiring familiarity with the antihistamines and their relative advantages in the various forms of urticaria. Elimination diets are of diagnostic as well as therapeutic value: pencillin-free, yeast-free, and salicylate-free diets are particularly useful. Therapeutic trials of tetracycline, nystatin and griseofulvin may be helpful, while corticosteroids and specific desensitization are rarely of value." }, "ArticleTitle": "Urticaria.", "AuthorList": { "Author": { "LastName": [ "Stone" ], "ForeName": [ "S P" ], "Initials": [ "SP" ], "CollectiveName": [ "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "BB/C008219/1" ], "Agency": [ "Biotechnology and Biological Sciences Research Council" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Review" ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0" ], "NameOfSubstance": [ "Histamine H1 Antagonists" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Histamine H1 Antagonists", "Humans", "Urticaria" ], "QualifierName": [ "therapeutic use", "", "diagnosis" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "7633" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1975, 1975, 1975 ], "Month": [ 12, 12, 12 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 8211, "DateCompleted": { "Year": 1976, "Month": 11, "Day": 1 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 7, "Day": 5 }, "Article": { "Abstract": { "AbstractText": "We have studied the mechanism of the specific inhibition of ribosomal RNA synthesis by ppGpp in a purified system using as templates E. coli DNA and DNA from lambdad5ilv, which carries a rRNA cistron from E. coli. Ribosomal RNA synthesis, as well as its inhibition by ppGpp, are critically salt-dependent. Of a number of guanosine phosphates tested, only pppGpp (MS II) mimicked the action of ppGpp, establishing the specificity of ppGpp. The two templates gave similar results for rRNA synthesis in all experiments. By using the initiation inhibitor rifampicin, we could show that the specific inhibition of rRNA synthesis by ppGpp is due to its effect on rRNA initiation. The somewhat variable inhibition of RNA synthesis in general by ppGpp is mainly or wholly a consequence of premature chain termination. We propose that ppGpp specifically inhibits rRNA synthesis by acting on the formation of the so-called \"closed-promoter complex\"." }, "ArticleTitle": "The mechanism of action of ppGpp on rRNA synthesis in vitro.", "AuthorList": { "Author": { "LastName": [ "van Ooyen", "Gruber", "Jorgensen" ], "ForeName": [ "A J", "M", "P" ], "Initials": [ "AJ", "M", "P" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "095938" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "660YQ98I10" ], "NameOfSubstance": [ "Guanine Nucleotides", "RNA, Bacterial", "RNA, Ribosomal", "Potassium Chloride" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Cell-Free System", "Coliphages", "Escherichia coli", "Guanine Nucleotides", "Hydrogen-Ion Concentration", "Potassium Chloride", "RNA, Bacterial", "RNA, Ribosomal", "Temperature" ], "QualifierName": [ "", "metabolism", "metabolism", "pharmacology", "", "pharmacology", "biosynthesis", "biosynthesis", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "8211", "0092-8674(76)90193-8", "10.1016/0092-8674(76)90193-8" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1976, 1976, 1976 ], "Month": [ 5, 5, 5 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 16877, "DateCompleted": { "Year": 1977, "Month": 7, "Day": 18 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 5, "Day": 9 }, "Article": { "Abstract": { "AbstractText": "As previously reported when a specific thiol group, S2, of myosin reacts with N-ethylmaleimide (NEM), its Ca2+-ATPase activity is decreased. Therefore, the reactivity of S2 can be estimated by measuring the decrement of the enzymatic activity. Using the change in the reactivity as a structural probe, we investigated whether F-actin affects the conformation around the region containing S2 under physiological conditions (at neutral pH and low ionic strength). 1. Experiments were carried out with heavy meromyosin (HMM), S1 of which had heen blocked with NEM, to observe the reactivity of S2 alone. In the experiments done in the presence of F-actin, the Ca2+-ATPase activity was measured using the heavy meromyosin fraction after actin had been removed by centrifugation and gel filtration. 2. ATP and other nucleotides activated the reactivity of S2 in the presence of Mg2+. On the other hand, F-actin markedly activated the reactivity of S2 which had been increased by ATP, but not by the other nucleotides. 3. The above cooperative action of F-actin with ATP was not observed in the presence of Ca2+ instead of Mg2+, or above 0.2 M KCl. These results suggest that the S2 region of the myosin molecule is a key region in the molecular interaction of the actin myosin-ATP system under physiological conditions." }, "ArticleTitle": "Actin-induced local conformational change in the myosin molecule. I. Effect of metal ions and nucleotides on the conformational change around a specific thiol group (S2) of heavy meromyosin.", "AuthorList": { "Author": { "LastName": [ "Kameyama", "Katori", "Sekine" ], "ForeName": [ "T", "T", "T" ], "Initials": [ "T", "T", "T" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "095495" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "61D2G4IYVH", "660YQ98I10", "8L70Q75FXE", "EC 3.6.1.-", "EC 3.6.4.1", "O3C74ACM9V", "SY7Q814VUP" ], "NameOfSubstance": [ "Actins", "Myosin Subfragments", "Ribonucleotides", "Adenosine Diphosphate", "Potassium Chloride", "Adenosine Triphosphate", "Adenosine Triphosphatases", "Myosins", "Ethylmaleimide", "Calcium" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Actins", "Adenosine Diphosphate", "Adenosine Triphosphatases", "Adenosine Triphosphate", "Animals", "Calcium", "Enzyme Activation", "Ethylmaleimide", "Hydrogen-Ion Concentration", "Kinetics", "Myosin Subfragments", "Myosins", "Osmolar Concentration", "Potassium Chloride", "Protein Conformation", "Rabbits", "Ribonucleotides" ], "QualifierName": [ "physiology", "pharmacology", "metabolism", "pharmacology", "", "pharmacology", "", "pharmacology", "", "", "metabolism", "metabolism", "", "pharmacology", "", "", "pharmacology" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "16877", "10.1093/oxfordjournals.jbchem.a131508" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1977, 1977, 1977 ], "Month": [ 3, 3, 3 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 16889, "DateCompleted": { "Year": 1977, "Month": 7, "Day": 23 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2021, "Month": 2, "Day": 10 }, "Article": { "Abstract": { "AbstractText": "The activity of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase, EC 1.1.1.34) has been demonstrated both in homogenates and microsomes of the S3G strain of HeLa cells. It was increased 8- to 10-fold by the removal of serum from the growth medium. The presence of steroids, specifically of the glucocorticoid series, in the serum-less growth medium elicited an additional 100 to 345% increase over the serum-less control, whereas the addition of N6,O2'-dibutyryl adenosine 3':5'-monophosphate to the medium or dexamethasone to the assay mixture was without any stimulatory effect. Both inductions were blocked by cycloheximide and actinomycin D, suggesting a protein synthesis-dependent elevation of enzyme activity. Glucocorticoids were effective in the induction at concentrations ranging from 10(-6) to 10(-8) M and there was a demonstrated parallel between the magnitude of enzyme induction and glucocorticoid potency. The HMG-CoA reductase activities from steroid-induced and control cultures had identical assay characteristics (pH optima and apparent Km values for both NADPH and HMG-CoA). This induction of the rate-controlling enzyme of cholesterogenesis occurred despite the observation that glucocorticoids specifically depress the rate of acetate or water, but not mevalonate, incorporation into cholesterol." }, "ArticleTitle": "Induction of 3-hydroxy-3-methylglutaryl coenzyme A reductase in HeLa cells by glucocorticoids.", "AuthorList": { "Author": { "LastName": [ "Cavenee", "Melnykovych" ], "ForeName": [ "W K", "G" ], "Initials": [ "WK", "G" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "095495" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, Non-P.H.S.", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "1CC1JFE158", "7S5I7G3JQL", "98600C0908", "EC 1.1.-", "EC 1.1.1.-" ], "NameOfSubstance": [ "Culture Media", "Glucocorticoids", "Sterols", "Dactinomycin", "Dexamethasone", "Cycloheximide", "Alcohol Oxidoreductases", "Hydroxymethylglutaryl CoA Reductases" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Alcohol Oxidoreductases", "Blood", "Culture Media", "Cycloheximide", "Dactinomycin", "Dexamethasone", "Enzyme Induction", "Glucocorticoids", "HeLa Cells", "Hydrogen-Ion Concentration", "Hydroxymethylglutaryl CoA Reductases", "Kinetics", "Sterols", "Structure-Activity Relationship" ], "QualifierName": [ "biosynthesis", "", "", "pharmacology", "pharmacology", "pharmacology", "drug effects", "pharmacology", "enzymology", "", "biosynthesis", "", "biosynthesis", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "16889", "S0021-9258(17)40383-8" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1977, 1977, 1977 ], "Month": [ 5, 5, 5 ], "Day": [ 25, 25, 25 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 17673, "DateCompleted": { "Year": 1977, "Month": 8, "Day": 12 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 7, "Day": 10 }, "Article": { "Abstract": { "AbstractText": "The central hypotensive action of clonidine, infused into the vertebral artery of chloralose-anaesthetized cats was antagonized by several phenothiazine-neuroleptics (chlorpromazine, promazine, promethazine, thiethylperazine, thioridazine), by chlorprothixene and to a limited extent by haloperidol administered via the same route. Pimozide and some benzodiazepines (chlordiazepoxide, diazepam and flurazepam) hardly influenced the central hypotensive response to clonidine. The antagonism between clonidine and the psychotropic drugs is probably associated with central alpha-adrenoceptors, clonidine being the agonist and the neuroleptic agents the antagonists at these receptors. Virtually the same type of antagonism was observed in conscious, spontaneously hypertensive rats where both clonidine and the neuroleptic drugs were injected intravenously. The phenothiazines and also piperoxane effectively diminished the centrally induced hypotensive response to clonidine, whereas the initial pressor effect to clonidine was not reduced." }, "ArticleTitle": "The interaction between clonidine and various neuroleptic agents and some benzodiazepine tranquillizers.", "AuthorList": { "Author": { "LastName": [ "van Zwieten" ], "ForeName": [ "P A" ], "Initials": [ "PA" ], "CollectiveName": [ "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "089701" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "12794-10-4", "238BZ29MUE", "MN3L5RMN02" ], "NameOfSubstance": [ "Anti-Anxiety Agents", "Antipsychotic Agents", "Benzodiazepines", "Chloralose", "Clonidine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Anesthesia", "Animals", "Anti-Anxiety Agents", "Antipsychotic Agents", "Benzodiazepines", "Blood Pressure", "Cats", "Chloralose", "Clonidine", "Drug Interactions", "Female", "Hypertension", "Male", "Rats", "Rats, Inbred Strains", "Time Factors" ], "QualifierName": [ "", "", "pharmacology", "pharmacology", "", "drug effects", "", "", "pharmacology", "", "", "physiopathology", "", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "17673", "10.1111/j.2042-7158.1977.tb11294.x" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1977, 1977, 1977 ], "Month": [ 4, 4, 4 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 21188, "DateCompleted": { "Year": 1977, "Month": 12, "Day": 29 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2021, "Month": 2, "Day": 10 }, "Article": { "Abstract": { "AbstractText": "The adenylate energy charge of human ejaculated spermatozoa was studied when the sperm motility was perturbed by varying pH, prolonged incubation, and caffeine. Between pH 8 and 9, which was optimal for the sperm motility, the energy charge was in the physiological range of 0.8 to 0.9. Above pH 9, the mobility, ATP content, and adenine nucleotide pool declined rapidly but the energy charge was maintained slightly below 0.8. Below pH 8, the motility also dropped drastically, but the ATP, nucleotide pool, and energy charge fell only slightly. Prolonged incubations of the spermatozoa decreased the motility, ATP, and nucleotide pool. However, the energy charge would remain above 0.6. Caffeine stimulation of the motility caused a rapid fall of ATP and the reduction of the physiological energy charge by 0.2 unit, unless glucose was added. Imidazole which reduced the caffeine-stimulated motility did not alter the physiological energy charge of the spermatozoa. The study showed that the spermatozoa could maintain the energy charge above 0.6 under stress." }, "ArticleTitle": "Stabilization of adenylate energy charge and its relation to human sperm motility.", "AuthorList": { "Author": { "LastName": [ "Chulavatnatol", "Haesungcharern" ], "ForeName": [ "M", "A" ], "Initials": [ "M", "A" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "BB/D008336/1" ], "Agency": [ "Biotechnology and Biological Sciences Research Council" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "3G6A5W338E", "IY9XDZ35W2" ], "NameOfSubstance": [ "Adenine Nucleotides", "Caffeine", "Glucose" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adenine Nucleotides", "Caffeine", "Energy Metabolism", "Glucose", "Humans", "Hydrogen-Ion Concentration", "Male", "Sperm Motility", "Spermatozoa" ], "QualifierName": [ "metabolism", "pharmacology", "", "pharmacology", "", "", "", "drug effects", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "21188", "S0021-9258(17)40941-0" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1977, 1977, 1977 ], "Month": [ 11, 11, 11 ], "Day": [ 25, 25, 25 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 21390, "DateCompleted": { "Year": 1977, "Month": 12, "Day": 29 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2020, "Month": 12, "Day": 9 }, "Article": { "Abstract": { "AbstractText": "The pH effect on the nisine biosynthesis during the cultivation of Streptococcus lactis was studied at pH 5,8 6,7 and 7,2. The pH maintenance at the specified level did not stimulate the growth of Str. lactis, did not increase the total yield of nisine and did not produce a significant effect on the level or cellular nisine. This indicates an important physiological difference between the culture-nisine producer described by Hirsh and our culture Str. lactis, str. Moscow University." }, "ArticleTitle": "[Influence of pH on nisin production by Streptococcus lactis cultures].", "AuthorList": { "Author": { "LastName": [ "Baranova", "Egorov", "Grushina" ], "ForeName": [ "I P", "N S", "V A" ], "Initials": [ "IP", "NS", "VA" ], "CollectiveName": [ "", "", "" ] } }, "Language": "rus", "GrantList": { "Grant": { "GrantID": [ "089701" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Comparative Study", "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "Russia (Federation)" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "1414-45-5" ], "NameOfSubstance": [ "Nisin" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Hydrogen-Ion Concentration", "Lactococcus lactis", "Nisin" ], "QualifierName": [ "", "metabolism", "biosynthesis" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "21390" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1977, 1977, 1977 ], "Month": [ 9, 9, 9 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 27707, "DateCompleted": { "Year": 1978, "Month": 9, "Day": 29 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2020, "Month": 12, "Day": 9 }, "Article": { "Abstract": { "AbstractText": "The effect of copper ions and unfavourable pH values of the medium on the incorporation of labelled precursors of protein and RNA was studied in Candida utilis. Specific inhibition of protein synthesis by copper ions and alkaline conditions was found. No specific inhibition of protein or RNA was detected at low pH values of the medium." }, "ArticleTitle": "[Action of copper ions and of unfavorable medium pH values on protein and RNA synthesis by Candida utilis cells].", "AuthorList": { "Author": { "LastName": [ "Khovrychev", "Korolev", "Bulgakova" ], "ForeName": [ "M P", "P N", "V G" ], "Initials": [ "MP", "PN", "VG" ], "CollectiveName": [ "", "", "" ] } }, "Language": "rus", "GrantList": { "Grant": { "GrantID": [ "089701" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "Russia (Federation)" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "56HH86ZVCT", "63231-63-0", "789U1901C5", "GMW67QNF9C" ], "NameOfSubstance": [ "Culture Media", "Fungal Proteins", "Ions", "Uracil", "RNA", "Copper", "Leucine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Candida", "Copper", "Culture Media", "Fungal Proteins", "Hydrogen-Ion Concentration", "Ions", "Leucine", "RNA", "Uracil" ], "QualifierName": [ "drug effects", "pharmacology", "pharmacology", "biosynthesis", "", "", "metabolism", "biosynthesis", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "27707" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 5, 5, 5 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 28118, "DateCompleted": { "Year": 1978, "Month": 9, "Day": 25 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 9, "Day": 2 }, "Article": { "Abstract": { "AbstractText": "Glutamine-dependent CPSase, ATCase, and DHOase from Drosophila, the first three enzymes in pyrimidine biosynthesis, show coordinate variation in activity throughout development. The three activities were highest in first instar larvae and decreased as development proceeded. The three activities cosediment in sucrose gradients as a single peak with a relative sedimentation coefficient of approximately 30S. CPSase, ATCase, and DHOase copurify during (NH4)2SO4 fractionation and during DEAE-cellulose and hydroxylapatite chromatography." }, "ArticleTitle": "Rudimentary locus of Drosophila melanogaster: partial purification of a carbamylphosphate synthase--aspartate transcarbamylase--dihydroorotase complex.", "AuthorList": { "Author": { "LastName": [ "Brothers", "Tsubota", "Germeraad", "Fristrom" ], "ForeName": [ "V M", "S I", "S E", "J W" ], "Initials": [ "VM", "SI", "SE", "JW" ], "CollectiveName": [ "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "089701" ], "Agency": [ "Wellcome Trust" ], "Country": [ "United Kingdom" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, Non-P.H.S.", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "EC 2.1.3.2", "EC 2.7.-", "EC 3.5.-", "EC 3.5.2.3", "EC 6.3.5.5" ], "NameOfSubstance": [ "Multienzyme Complexes", "Aspartate Carbamoyltransferase", "Phosphotransferases", "Amidohydrolases", "Dihydroorotase", "Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Amidohydrolases", "Animals", "Aspartate Carbamoyltransferase", "Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)", "Dihydroorotase", "Drosophila melanogaster", "Multienzyme Complexes", "Phosphotransferases" ], "QualifierName": [ "genetics", "", "genetics", "genetics", "genetics", "enzymology", "genetics", "genetics" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "28118", "10.1007/BF00484088" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 4, 4, 4 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 31907, "DateCompleted": { "Year": 1979, "Month": 3, "Day": 24 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 6, "Day": 12 }, "Article": { "Abstract": { "AbstractText": "The acyl-carrier protein (ACP) of Escherichia coli is a protein of molecular weight 8847 with a 4'-phosphopanthetheine prosthetic group. ACP functions (via the SH of the prosthetic group) as a coenzyme in the synthesis of fatty acids and complex lipids. We report proton nuclear magnetic resonance (NMR) studies of the structure of ACP under various experimental conditions. The motion of the fatty acyl chain of acyl-ACP has been investigated by 19FNMR studies of difluorotetradecanoyl-ACP. 31PNMR studies of the prosthetic group phosphorus of ACP and acyl-ACP are also reported. We make the following conclusions: (1) the structure of ACP is stabilized by surface charge, and (2) the fatty acid residue of acyl-ACP does not move freely and seems immobilized by an interaction with the protein moiety." }, "ArticleTitle": "Acyl carrier protein from Escherichia coli: characterization by proton and fluorine-19 nuclear magnetic resonance and evidence for restricted mobility of the fatty acid chain in tetradecanoyl-acyl-carrier protein.", "AuthorList": { "Author": { "LastName": [ "Gally", "Spencer", "Armitage", "Prestegard", "Cronan" ], "ForeName": [ "H U", "A K", "I M", "J H", "J E" ], "Initials": [ "HU", "AK", "IM", "JH", "JE" ], "CollectiveName": [ "", "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "R01 AI015650" ], "Agency": [ "NIAID NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "42HK56048U" ], "NameOfSubstance": [ "Acyl Carrier Protein", "Fatty Acids", "Tyrosine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Acyl Carrier Protein", "Escherichia coli", "Fatty Acids", "Hydrogen-Ion Concentration", "Magnetic Resonance Spectroscopy", "Protein Conformation", "Temperature", "Tyrosine" ], "QualifierName": [ "", "analysis", "analysis", "", "", "", "", "analysis" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "31907", "10.1021/bi00618a009" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 2001, 1978 ], "Month": [ 12, 3, 12 ], "Day": [ 12, 28, 12 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 32653, "DateCompleted": { "Year": 1979, "Month": 3, "Day": 13 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 10, "Day": 21 }, "Article": { "Abstract": { "AbstractText": "The axial projection of the glutamine synthetase molecule has been reconstructed from electron micrographs of a stained preparation by using a new method of correlation search and averaging. The average over 50 individual molecules appears as a radial pattern with sixfold symmetry. The handedness evident in the average is attributed to nonuniformity of the negative stain." }, "ArticleTitle": "Reconstruction of glutamine synthetase using computer averaging.", "AuthorList": { "Author": { "LastName": [ "Frank", "Goldfarb", "Eisenberg", "Baker" ], "ForeName": [ "J", "W", "D", "T S" ], "Initials": [ "J", "W", "D", "TS" ], "CollectiveName": [ "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "" ], "Agency": [ "Howard Hughes Medical Institute" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article" ] } }, "MedlineJournalInfo": { "Country": "Netherlands" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "EC 6.3.1.2" ], "NameOfSubstance": [ "Glutamate-Ammonia Ligase" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Bacillus", "Computers", "Glutamate-Ammonia Ligase", "Microscopy, Electron", "Protein Conformation" ], "QualifierName": [ "enzymology", "", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "32653", "PMC4167717", "HHMIMS620907", "10.1016/s0304-3991(78)80038-2" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 41808, "DateCompleted": { "Year": 1980, "Month": 2, "Day": 28 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2018, "Month": 11, "Day": 13 }, "Article": { "Abstract": { "AbstractText": "A simple, reproducible and quantitative method for evaluating certain non-specific immunological inhibitors in a variety of biological fluids is described. Human lymphocytes were stimulated with PHA in the presence of colchicine. Phytohaemagglutinin stimulated a large percentage of cells and colchicine's selective blockage of mitosis limited the stimulated cells to one S phase. These conditions effectively established a maximum amount of DNA synthesis within each culture. Quantification of suppression was then achieved by measuring a decrease from this maximum. The PHA-colchicine assay was successfully used to quantify inhibition by normal plasma, normal mouse sera, mouse neonate sera, murine Ehrlich's and sarcoma I ascitic fluids and an immunoregulatory alpha-globulin peptide preparation. Because of the ability to obtain a specific inhibitory activity for the suppressive factors, this assay was particularly suited for following the isolation of inhibitors during the fractionation of suppressive substances from complex fluids." }, "ArticleTitle": "Quantification of non-specific immunosuppressive factors.", "AuthorList": { "Author": { "LastName": [ "Anderson", "Tomasi" ], "ForeName": [ "W L", "T B" ], "Initials": [ "WL", "TB" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "R01 HD017013" ], "Agency": [ "NICHD NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "SML2Y3J35T", "VC2W18DGKR" ], "NameOfSubstance": [ "Immunosuppressive Agents", "Peptides", "Phytohemagglutinins", "Colchicine", "Thymidine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Animals", "Ascitic Fluid", "Biological Assay", "Blood", "Carcinoma, Ehrlich Tumor", "Colchicine", "Humans", "Hydrogen-Ion Concentration", "Immunosuppressive Agents", "Lymphocytes", "Mice", "Peptides", "Phytohemagglutinins", "Sarcoma, Experimental", "Thymidine", "Time Factors" ], "QualifierName": [ "", "immunology", "methods", "", "immunology", "pharmacology", "", "", "analysis", "drug effects", "", "immunology", "pharmacology", "immunology", "metabolism", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "41808", "PMC1457891" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 2001, 1979 ], "Month": [ 9, 3, 9 ], "Day": [ 1, 28, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45081, "DateCompleted": { "Year": 1980, "Month": 11, "Day": 24 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 9, "Day": 2 }, "Article": { "Abstract": { "AbstractText": "Benzodiazepine derivatives are the most commonly prescribed anti-anxiety agents in clinical practice. Six benzodiazepine anxiolytics are now available in the United States. Additional drugs are used in other parts of the world, and many others are in various stages of clinical testing. All these benzodiazepine derivatives have similar neuropharmacological properties--they reduce anxiety, produce sedation and sleep, have anticonvulsant effects, and can produce muscle relaxation. Faced with this bewildering array of drugs from the same class which are very similar in intrinsic effects upon the brain, the clinician may well ask how best to make a rational choice among the available derivatives. Despite neuropharmacological similarities, there are differences among benzodiazepines in patterns of absorption, distribution, and elimination by the human body. These pharmacokinetic differences may in turn lead to apparent differences in clinical action. This review summarizes pertinent pharmacokinetic characteristics of benzodiazepine anti-anxiety agents." }, "ArticleTitle": "Benzodiazepines: some aspects of their clinical pharmacology.", "AuthorList": { "Author": { "LastName": [ "Shader", "Greenblatt" ], "ForeName": [ "R I", "D J" ], "Initials": [ "RI", "DJ" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "MH-12279" ], "Agency": [ "NIMH NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, Non-U.S. Gov't", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "Netherlands" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "63FN7G03XY", "6GOW6DWN2A", "6RZ6XEZ3CR", "O26FZP769L", "Q30VCC064M", "Q3JTX2Q7TU" ], "NameOfSubstance": [ "Anti-Anxiety Agents", "Clorazepate Dipotassium", "Oxazepam", "Chlordiazepoxide", "Lorazepam", "Prazepam", "Diazepam" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Anti-Anxiety Agents", "Chlordiazepoxide", "Clorazepate Dipotassium", "Diazepam", "Humans", "Lorazepam", "Oxazepam", "Prazepam" ], "QualifierName": [ "therapeutic use", "therapeutic use", "therapeutic use", "therapeutic use", "", "therapeutic use", "therapeutic use", "therapeutic use" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45081", "10.1002/9780470720578.ch9" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45127, "DateCompleted": { "Year": 1980, "Month": 11, "Day": 25 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 8, "Day": 23 }, "Article": { "Abstract": { "AbstractText": "The awareness of extrapyramidal reactions during initiation of neuroleptic treatment was studied in 14 patients. Only one patient spontaneously identified the presence of dystonia. The other 13, including 3 who had experienced extrapyramidal reactions during previous hospitalizations, did not fully identify the presence of symptoms, although several had vague discomfort. There was marked variability in acknowledgement of symptoms in response to prompting by staff members. The findings are similar to reports of agnosia for hemiparesis after parietal lobe injury and also to descriptions of agnosia in animals caused by destruction of dopaminergic neurons. Since extrapyramidal reactions represent blockade of dopaminergic neurotransmission, patients' inability to perceive the reactions may represent evidence for catecholaminergic modulation of sensory perception." }, "ArticleTitle": "Patients' awareness of extrapyramidal reactions to neuroleptic drugs: possible evidence for the role of catecholamines in perception.", "AuthorList": { "Author": { "LastName": [ "Freedman", "Silverman", "Schwab" ], "ForeName": [ "R", "M M", "P J" ], "Initials": [ "R", "MM", "PJ" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "NS-09199-09" ], "Agency": [ "NINDS NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "Ireland" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "VTD58H1Z2X" ], "NameOfSubstance": [ "Antipsychotic Agents", "Dopamine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adolescent", "Adult", "Antipsychotic Agents", "Awareness", "Basal Ganglia Diseases", "Cognition", "Dopamine", "Dystonia", "Female", "Humans", "Male", "Middle Aged", "Perception", "Psychotic Disorders" ], "QualifierName": [ "", "", "adverse effects", "", "chemically induced", "", "physiology", "chemically induced", "", "", "", "", "physiology", "psychology" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45127", "0165-1781(79)90025-8", "10.1016/0165-1781(79)90025-8" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 7, 7, 7 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45130, "DateCompleted": { "Year": 1980, "Month": 11, "Day": 24 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 8, "Day": 23 }, "Article": { "Abstract": { "AbstractText": "Neuroendocrine studies that examine the changes in serum prolactin levels following intramuscular (im) neuroleptics have usually monitored prolactin levels before and for 90 minutes to 3 hours after neuroleptic injection. Recent studies have suggested that this may be an inadequate period of time. In the present study, six male and four female psychiatric inpatients, who had not received neuroleptic medication for at least 1 week before the study began, received an injection of chlorpromazine (CPZ) 25 mg im; serum prolactin levels were monitored for 6 hours after injection. Peak serum prolactin levels occurred at 60 minutes in one subject, 90 minutes in three subjects, 120 minutes in two subjects, 180 minutes in three subjects, and 240 minutes in one subject. Area under the serum prolactin curve at 2 hours and area under the curve at 3 hours after CPZ injection were found to be good predictors (r = 0.86; r = 0.95, respectively) of 6-hour area under the curve. Two-hour studies should therefore not be considered inadequate; however, a 3-hour study length results in more precise characterization of prolactin response to im CPZ." }, "ArticleTitle": "Serum prolactin levels following intramuscular chlorpromazine: two- and three-hour response as predictors of six-hour response.", "AuthorList": { "Author": { "LastName": [ "Busch", "Fang", "Meltzer" ], "ForeName": [ "D A", "V S", "H Y" ], "Initials": [ "DA", "VS", "HY" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "MH RCSA MH-47,808", "MH-29,206", "MH-30,936" ], "Agency": [ "NIMH NIH HHS", "NIMH NIH HHS", "NIMH NIH HHS" ], "Country": [ "United States", "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "Ireland" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "9002-62-4", "U42B7VYA4P" ], "NameOfSubstance": [ "Antipsychotic Agents", "Prolactin", "Chlorpromazine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Acute Disease", "Adolescent", "Adult", "Antipsychotic Agents", "Chlorpromazine", "Chronic Disease", "Depressive Disorder", "Female", "Humans", "Injections, Intramuscular", "Male", "Middle Aged", "Prolactin", "Schizophrenia", "Time Factors" ], "QualifierName": [ "", "", "", "administration & dosage", "administration & dosage", "", "blood", "", "", "", "", "", "blood", "blood", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45130", "0165-1781(79)90056-8", "10.1016/0165-1781(79)90056-8" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 10, 10, 10 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45131, "DateCompleted": { "Year": 1980, "Month": 11, "Day": 24 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 8, "Day": 23 }, "Article": { "Abstract": { "AbstractText": "Chlorpromazine and thioridazine are widely used antipsychotic agents that are extensively metabolized. Parent compounds and metabolites have diverse pharmacologic activities, and differences in patterns of metabolism may explain differences in therapeutic and side effects from individual to individual. Radioreceptor assays were used to determine the neuroleptic, antimuscarinic, and anti-alpha-noradrenergic potency of chlorpromazine, thioridazine, and their metabolites. The results indicate that these metabolites show a wide range of potencies. The spectrum of activity of a metabolite may be quite different from that of its parent compound. The clinical relevance of these findings to individual differences in drug response is discussed. The combined use of radioreceptor assays and chemical assays in future clinical research is proposed." }, "ArticleTitle": "Neuroleptic, antimuscarinic, and antiadrenergic activity of chlorpromazine, thioridazine, and their metabolites.", "AuthorList": { "Author": { "LastName": [ "Cohen", "Herschel", "Aoba" ], "ForeName": [ "B M", "M", "A" ], "Initials": [ "BM", "M", "A" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "MH-30511", "MH-31154" ], "Agency": [ "NIMH NIH HHS", "NIMH NIH HHS" ], "Country": [ "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, Non-U.S. Gov't", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "Ireland" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "N3D6TG58NI", "U42B7VYA4P" ], "NameOfSubstance": [ "Antipsychotic Agents", "Parasympatholytics", "Sympatholytics", "Thioridazine", "Chlorpromazine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Animals", "Antipsychotic Agents", "Cattle", "Chlorpromazine", "In Vitro Techniques", "Parasympatholytics", "Radioligand Assay", "Sympatholytics", "Thioridazine" ], "QualifierName": [ "", "pharmacology", "", "analogs & derivatives", "", "pharmacology", "", "pharmacology", "analogs & derivatives" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45131", "0165-1781(79)90062-3", "10.1016/0165-1781(79)90062-3" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 10, 10, 10 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45219, "DateCompleted": { "Year": 1981, "Month": 1, "Day": 16 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2020, "Month": 8, "Day": 25 }, "Article": { "Abstract": { "AbstractText": "We have isolated temperature resistant revertants from temperature sensitive E. coli strains containing either a thermolabile glutaminyl-tRNA synthetase or leucyl-tRNA synthetase. Among the revertants which still contained the thermolabile leucyl-tRNA synthetase we found two classes of regulatory mutants (leuX and leu Y) which have elevated levels of this enzyme. The leuX mutation specifies an operator-promoter region adjacent to the structural gene (leuS) for the enzyme. The leuY gene maps away from the leuS gene and codes for a protein. Using these mutants we demonstrated that the levels of leucyl-tRNA are related to the derepression of the leucine and isoleucine-valine operons. Among the revertants which still contained the thermolabile glutaminyl-tRNA synthetase were characterized three classes of mutants, glnT, glnU, and glnR. The glnT and glnU mutants contain elevated levels of tRNAgln, while the glnR mutant possesses elevated levels of glutaminyl-tRNA synthetase. The level of glutamine synthetase, the enzyme responsible for the formation of glutamine, is also derepressed in the glnT and glnR mutants." }, "ArticleTitle": "Regulation of biosynthesis of aminoacyl-transfer RNA synthetases and of transfer-RNA in Escherichia coli.", "AuthorList": { "Author": { "LastName": [ "Morgan", "Larossa", "Cheung", "Low", "Söll" ], "ForeName": [ "S", "R", "A", "B", "D" ], "Initials": [ "S", "R", "A", "B", "D" ], "CollectiveName": [ "", "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "CA06519", "GM22854", "HD09167" ], "Agency": [ "NCI NIH HHS", "NIGMS NIH HHS", "NICHD NIH HHS" ], "Country": [ "United States", "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "Chile" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "9014-25-9", "EC 6.1.1.-", "EC 6.1.1.4", "EC 6.3.1.2" ], "NameOfSubstance": [ "RNA, Transfer, Amino Acyl", "RNA, Transfer", "Amino Acyl-tRNA Synthetases", "Leucine-tRNA Ligase", "Glutamate-Ammonia Ligase" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Amino Acyl-tRNA Synthetases", "Chromosome Mapping", "Escherichia coli", "Gene Expression Regulation", "Genes, Regulator", "Glutamate-Ammonia Ligase", "Leucine-tRNA Ligase", "Mutation", "Operon", "RNA, Transfer", "RNA, Transfer, Amino Acyl", "Temperature" ], "QualifierName": [ "biosynthesis", "", "genetics", "", "", "genetics", "genetics", "", "", "biosynthesis", "genetics", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45219" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 10, 10, 10 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45221, "DateCompleted": { "Year": 1981, "Month": 2, "Day": 26 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2013, "Month": 11, "Day": 21 }, "Article": { "Abstract": { "AbstractText": "As a function of buffer pH, [125I]-insulin binding to rat mammary cells, rat adipocytes, or membranes prepared therefrom, at 4 degrees or 20 degrees C, showed 2 peaks in different buffers. Specific insulin binding at the pH 7.7. peak (100 +/- 11%) was lower than at pH 8.8 (140 +/- 17%) with no change in nonspecific binding. Although insulin stimulation of glucose uptake into fat cells was highest at pH 7.5, this response was also seen at pH 8.6. Scatchard affinity profiles, or in the kinetics of dissociation. Insulin degradation (< 10%) and binding to insulin antibody were similar over the pH range of 7 to 9." }, "ArticleTitle": "Effect of pH and buffers on insulin binding to normal and neoplastic mammary cells, fat cells and membrane preparations.", "AuthorList": { "Author": { "LastName": [ "Shafie", "Cech", "Livingston", "Hilf" ], "ForeName": [ "S M", "J M", "J N", "R" ], "Initials": [ "SM", "JM", "JN", "R" ], "CollectiveName": [ "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "CA-11198", "CA-16660", "IF-32CA 05941" ], "Agency": [ "NCI NIH HHS", "NCI NIH HHS", "NCI NIH HHS" ], "Country": [ "United States", "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Comparative Study", "Journal Article", "Research Support, Non-U.S. Gov't", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "EC 2.7.10.1", "IY9XDZ35W2" ], "NameOfSubstance": [ "Insulin", "Receptor, Insulin", "Glucose" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adenocarcinoma", "Adipose Tissue", "Animals", "Biological Transport, Active", "Cell Membrane", "Female", "Glucose", "Hydrogen-Ion Concentration", "Insulin", "Kinetics", "Mammary Glands, Animal", "Mammary Neoplasms, Experimental", "Rats", "Receptor, Insulin" ], "QualifierName": [ "metabolism", "drug effects", "", "drug effects", "metabolism", "", "metabolism", "", "metabolism", "", "metabolism", "metabolism", "", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45221" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45223, "DateCompleted": { "Year": 1981, "Month": 2, "Day": 19 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 10, "Day": 21 }, "Article": { "Abstract": { "AbstractText": "Bicarbonate was found to stimulate ATP breakdown by rabbit or cat ciliary body-iris homogenates. Maximum HCO3- stimulation of ATPase with Tris-Hepes buffer occured at pH 8.0. Acid pH and chloride ions in the media reduced the activity of the HCO3--stimulated ATPase. The Km for ATP was 0.55 mmolar and for HCO3-, 20 mmlar. HCO3- ATPase was not inhibited by acetazolamide added to in vitro. It is postulated that ATPase represents the linkage step of energy donor mechanism and active CT secretion in acid aqueous humors (human, cat.) or HCO3- secretion in alkaline aqueous humor (rabbit, guinea pig). Inhibition of Cl- or HCO3- secretion by acetazolamide results from decreased intracellular HCO3- levels which, in turn, reduces the stimulation of the HCO3- ATPase." }, "ArticleTitle": "Bicarbonate ATP-ase in ciliary body and a theory of Diamox effect on aqueous humor formation.", "AuthorList": { "Author": { "LastName": [ "Cotlier" ], "ForeName": [ "E" ], "Initials": [ "E" ], "CollectiveName": [ "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "EY 02013" ], "Agency": [ "NEI NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "Netherlands" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "8L70Q75FXE", "EC 3.6.1.-", "O3FX965V0I" ], "NameOfSubstance": [ "Bicarbonates", "Chlorides", "Adenosine Triphosphate", "Adenosine Triphosphatases", "Acetazolamide" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Acetazolamide", "Adenosine Triphosphatases", "Adenosine Triphosphate", "Animals", "Aqueous Humor", "Bicarbonates", "Cats", "Chlorides", "Ciliary Body", "Guinea Pigs", "Humans", "Hydrogen-Ion Concentration", "In Vitro Techniques", "Iris", "Rabbits", "Uvea" ], "QualifierName": [ "pharmacology", "analysis", "pharmacology", "", "drug effects", "pharmacology", "", "", "enzymology", "", "", "", "", "enzymology", "", "enzymology" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45223", "10.1007/BF00154199" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 2, 2, 2 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45268, "DateCompleted": { "Year": 1981, "Month": 3, "Day": 17 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 7, "Day": 22 }, "Article": { "Abstract": { "AbstractText": "The relative contribution of the renin-angiotensin system, adenocorticotrophic hormone (ACTH) and plasma electrolytes in the response of plasma aldosterone to 30 minutes of 65 degrees head-up tilt was assessed in 10 essential hypertensive patients. Studies were carried out before and during acute blockade of renin release by propranolol, ACTH suppression by dexamethasone and combined renin and ACTH blockade. In control studies orthostasis induced significant increases only in plasma renin activity and aldosterone. In contrast, when the renin response to tilt was acutely suppressed by propranolol administration, the aldosterone response was nonetheless maintained but now appeared to be under ACTH control, since concurrent increases in cortisol were observed. During ACTH suppression aldosterone increased during tilt and so did renin. However, during combined ACTH and renin blockade aldosterone failed to increase during tilt. These studies suggest that the aldosterone secretory response to head-up tilt is normally mediated by the renin-angiotensin system but, when the renin response is suppressed, an ACTH response is elicited which assumes a backup role. However, when these two systems are blocked other factors appear unable to respond during tilt to support a normal aldosterone response." }, "ArticleTitle": "The substitutive role of ACTH in supporting aldosterone response to head-up tilt during acute renin suppression in patients with essential hypertension.", "AuthorList": { "Author": { "LastName": [ "Morganti", "Sealey", "Lopez-Ovejero", "Pickering", "Laragh" ], "ForeName": [ "A", "J E", "J A", "T G", "J H" ], "Initials": [ "A", "JE", "JA", "TG", "JH" ], "CollectiveName": [ "", "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "F05JW2455-02" ], "Agency": [ "PHS HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "4964P6T9RB", "9002-60-2", "EC 3.4.23.15" ], "NameOfSubstance": [ "Adrenergic beta-Antagonists", "Aldosterone", "Adrenocorticotropic Hormone", "Renin" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adrenergic beta-Antagonists", "Adrenocorticotropic Hormone", "Adult", "Aldosterone", "Blood Pressure", "Female", "Humans", "Hypertension", "Male", "Middle Aged", "Posture", "Renin" ], "QualifierName": [ "metabolism", "metabolism", "", "metabolism", "", "", "", "physiopathology", "", "", "", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45268", "10.1161/01.hyp.1.2.130" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 3, 3, 3 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45334, "DateCompleted": { "Year": 1981, "Month": 5, "Day": 13 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2014, "Month": 11, "Day": 20 }, "Article": { "Abstract": { "AbstractText": "Pulmonary mixed function oxidations are altered by in vivo exposure to paraquat or ozone. The cytochrome P-450-mediated benzphetamine N-demethylase activity was inhibited by low doses of both oxidants (paraquat, 20 mg/kg, ip; ozone, 1 ppm, 24 hrs). The effect of paraquat did not appear until 4 days after treatment and was still apparent after 2 weeks. The inhibition following exposure to ozone appeared immediately (1 day) and had resolved by one week. Cytochrome b5-mediated lipid desaturation was unaffected by the paraquat treatment and was stimulated by ozone. These alterations in pulmonary mixed function oxidase activities could not be explained by microsomal lipid peroxidation. The concentrations of cytochromes P450 and b5 also did not accurately reflect the altered enzymatic activities. The sites of the paraquat- and ozone-mediated alterations are still unknown." }, "ArticleTitle": "Oxidant-induced alterations in pulmonary microsomal mixed-function oxidation: acute effects of paraquat and ozone.", "AuthorList": { "Author": { "LastName": [ "Montgomery", "Niewoehner" ], "ForeName": [ "M R", "D E" ], "Initials": [ "MR", "DE" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "ESHL 01365" ], "Agency": [ "NIEHS NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Comparative Study", "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "66H7ZZK23N", "9035-39-6", "9035-51-2", "EC 1.-", "EC 1.-", "EC 1.14.14.1", "EC 1.14.19.1", "EC 1.5.-", "PLG39H7695" ], "NameOfSubstance": [ "Cytochromes", "Ozone", "Cytochromes b5", "Cytochrome P-450 Enzyme System", "Mixed Function Oxygenases", "Oxidoreductases", "benzphetamine N-demethylase", "Stearoyl-CoA Desaturase", "Oxidoreductases, N-Demethylating", "Paraquat" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Animals", "Cytochrome P-450 Enzyme System", "Cytochromes", "Cytochromes b5", "Dose-Response Relationship, Drug", "In Vitro Techniques", "Kinetics", "Lung", "Male", "Microsomes", "Mixed Function Oxygenases", "Oxidoreductases", "Oxidoreductases, N-Demethylating", "Ozone", "Paraquat", "Rats", "Stearoyl-CoA Desaturase" ], "QualifierName": [ "", "metabolism", "metabolism", "", "", "", "", "drug effects", "", "enzymology", "metabolism", "metabolism", "antagonists & inhibitors", "pharmacology", "pharmacology", "", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45334" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45353, "DateCompleted": { "Year": 1981, "Month": 6, "Day": 23 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2009, "Month": 11, "Day": 19 }, "Article": { "Abstract": { "AbstractText": "The circadian rhythms of sucrase, maltase, isomaltase, trehalase, lactase, gamma-glutamyltransferase, leucylnaphthylamide hydrolyzing activity, alkaline phosphatase and monosaccharide transport were assessed in each fifth of the small intestine of the rat in order to determine if an entire enzyme or transport system population responded in a similar manner or if there were regional differences. Animals were maintained under a light-dark cycle and fed from 1400-1800, EST for 7 days. Functional activities were assessed every 4 h for 24 h, inclusively. Quantitative, and in a few instances, qualitative differences in different areas of the intestine were found for all functions. There were portions of the lactase and alkaline phosphatase populations which displayed no rhythmicity in activity. When rhythmicity was observed there were differences in the activity patterns along the intestine for all functions. Thus, the rhythm patterns obtained from homogenates of the entire small intestine are a composite of the patterns in regions of high average activity. Also, there appears to be a reasonable amount of local control of the various functions." }, "ArticleTitle": "Regional variability in circadian rhythmicity of intestinal digestive-absorptive functions.", "AuthorList": { "Author": { "LastName": [ "Stevenson", "Sitren" ], "ForeName": [ "N R", "H S" ], "Initials": [ "NR", "HS" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "AM 05699", "AM 18953" ], "Agency": [ "NIADDK NIH HHS", "NIADDK NIH HHS" ], "Country": [ "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "EC 2.3.2.2", "EC 3.1.3.1", "EC 3.2.1.-", "EC 3.4.11.1" ], "NameOfSubstance": [ "Methylglucosides", "gamma-Glutamyltransferase", "Alkaline Phosphatase", "Glycoside Hydrolases", "Leucyl Aminopeptidase" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Alkaline Phosphatase", "Animals", "Circadian Rhythm", "Digestion", "Glycoside Hydrolases", "Intestinal Absorption", "Intestine, Small", "Kinetics", "Leucyl Aminopeptidase", "Male", "Methylglucosides", "Rats", "gamma-Glutamyltransferase" ], "QualifierName": [ "metabolism", "", "", "", "metabolism", "", "metabolism", "", "metabolism", "", "metabolism", "", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45353" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45395, "DateCompleted": { "Year": 1981, "Month": 10, "Day": 25 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 6, "Day": 6 }, "Article": { "Abstract": { "AbstractText": "The fluorescence parameters of ethenoadenosine derivatives are influenced by metal cations and pH, as summarized here. The pH profile of ethenoadenosine determined by fluorescence intensity gives a normal titration curve and is not affected by ionic strength. In contrast, the pH titration curves of etheno-ATP, etheno ADP, and etheno AMP depend upon ionic strength. At high ionic strength normal curves are obtained, whereas at low ionic strength anomalies are obtained; this suggests that the phosphates can interact with the ring, possibly by hydrogen binding to the ring nitrogens. The room temperature fluorescence of ethenoadenosine occurs from the base form, although excitation of either the acid or base forms can contribute to the emission. This result can be explained if the excited state pK is lower than the ground state pK, and if deprotonation occurs within the time scale of the excited state. At low pH values the fluorescence lifetime of the base form is dependent upon the buffer concentration, indicating that the reverse reaction, protonation, occurs. The affinity constants for the binding of metals to the ethenoadenosine phosphates resemble those for the corresponding adenosine phosphates. Ni(II) and Co(II) are more effective than Mn(II) in quenching the fluorescence of ethenoadenosine phosphates; this result is predicted by Förster's theory for energy transfer based upon the overlap between donor emission spectrum and acceptor absorption spectrum. The diamagnetic ions Mg(II), Ca(II), and Zn(II) do not appear to affect the fluorescence of the ethenoadenosine phosphates directly, but rather to affect the conformation of the molecule, thereby affecting the quantum yield." }, "ArticleTitle": "Fluorescent derivatives of nucleotides. Metal ion interactions and pH dependency.", "AuthorList": { "Author": { "LastName": [ "Vanderkooi", "Weiss", "Woodrow" ], "ForeName": [ "J M", "C J", "G V" ], "Initials": [ "JM", "CJ", "GV" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "5K04GM53", "GM12202", "GM21699" ], "Agency": [ "NIGMS NIH HHS", "NIGMS NIH HHS", "NIGMS NIH HHS" ], "Country": [ "United States", "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "0", "37482-16-9", "38806-39-2", "415SHH325A", "61D2G4IYVH", "8L70Q75FXE" ], "NameOfSubstance": [ "Cations", "Ethenoadenosine Triphosphate", "Fluorescent Dyes", "Metals", "etheno-AMP", "1,N(6)-ethenoadenosine diphosphate", "Adenosine Monophosphate", "Adenosine Diphosphate", "Adenosine Triphosphate" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adenosine Diphosphate", "Adenosine Monophosphate", "Adenosine Triphosphate", "Cations", "Chemical Phenomena", "Chemistry", "Ethenoadenosine Triphosphate", "Fluorescent Dyes", "Hydrogen-Ion Concentration", "Kinetics", "Mathematics", "Metals", "Spectrometry, Fluorescence" ], "QualifierName": [ "analogs & derivatives", "analogs & derivatives", "analogs & derivatives", "", "", "", "", "", "", "", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45395", "PMC1328463", "S0006-3495(79)85290-X", "10.1016/s0006-3495(79)85290-x" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 2, 2, 2 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45397, "DateCompleted": { "Year": 1981, "Month": 10, "Day": 29 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2018, "Month": 11, "Day": 13 }, "Article": { "Abstract": { "AbstractText": "A quasi-short-circuit (tunable voltage clamp) measurement method with microsecond time resolution was applied to a bacteriorhodopsin model membrane formed by a novel interfacial technique. A new component (B1) of the displacement photocurrent was recorded: it has no detectable latency at an instrumental time constant of 1.5 museconds, and persists at 5 degrees C. In addition, a slower component (B2) of opposite polarity inhibited by low temperature (5 degrees C) and low pH (pH = 3.0) was recorded. The technique is very sensitive for the study of fast capacitative photoresponses in model membranes, and allows the detection of charge displacements in bacteriorhodopsin associated with distinct stages of the photochemical transformation." }, "ArticleTitle": "Bacteriorhodopsin in model membranes. A new component of the displacement photocurrent in the microsecond time scale.", "AuthorList": { "Author": { "LastName": [ "Hong", "Montal" ], "ForeName": [ "F T", "M" ], "Initials": [ "FT", "M" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "EY-02084", "GM-25144", "RR-07011-12" ], "Agency": [ "NEI NIH HHS", "NIGMS NIH HHS", "NCRR NIH HHS" ], "Country": [ "United States", "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, Non-U.S. Gov't", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "36-88-4", "53026-44-1" ], "NameOfSubstance": [ "Membranes, Artificial", "Carotenoids", "Bacteriorhodopsins" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Bacteriorhodopsins", "Carotenoids", "Electric Conductivity", "Halobacterium", "Hydrogen-Ion Concentration", "Kinetics", "Membranes, Artificial", "Models, Biological", "Temperature", "Time Factors" ], "QualifierName": [ "metabolism", "metabolism", "", "metabolism", "", "", "", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45397", "PMC1328484", "S0006-3495(79)85316-3", "10.1016/S0006-3495(79)85316-3" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 3, 3, 3 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45400, "DateCompleted": { "Year": 1981, "Month": 10, "Day": 25 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2018, "Month": 11, "Day": 13 }, "Article": { "Abstract": { "AbstractText": "The effects of low pH, and of alkaline earth cations, were examined on calcium uptake by pinched-off nerve terminals (synaptosomes). This uptake appears to be mediated by voltage-sensitive Ca channels (J. Physiol. 247:617, 1975). Ca uptake was measured in low (5 mM) or high (77 mM) potassium media. The extra uptake promoted by depolarizing (K-rich) media was almost maximal at pH 7.5, and decreased as the pH was lowered. Data relating depolarization-induced 45Ca uptake to pH fit a titration curve with a pKa approximately 6. Experiments in which Ca concentration and pH were both varied indicated that Ca2+ and H+ compete for a common binding site. Inhibition of depolarization-induced 45Ca uptake by the alkaline earth cations was studied to determine the apparent binding sequence for these cations in the Ca channels: Ca greater than Sr greater than Ba greater than Mg. This sequence resembles that observed for block of Ca channels in other preparations. The apparent binding sequence of the alkaline earth cations and the apparent pKa (approximately 6) of the Ca-binding site indicate that the Ca channel is a \"high field strength\" system. Protonation of a Ca channel binding site could explain the inhibitory effect of low pH on Ca-dependent neurotransmitter release (cf. Del Castillo et al., J. Cell. Comp. Physiol. 59:35, 1962)." }, "ArticleTitle": "Regulation of nerve terminal calcium channel selectivity by a weak acid site.", "AuthorList": { "Author": { "LastName": [ "Nachshen", "Blaustein" ], "ForeName": [ "D A", "M P" ], "Initials": [ "DA", "MP" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "NS-08442" ], "Agency": [ "NINDS NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "RWP5GA015D", "SY7Q814VUP" ], "NameOfSubstance": [ "Cations, Divalent", "Ion Channels", "Potassium", "Calcium" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Animals", "Biological Transport, Active", "Brain", "Calcium", "Cations, Divalent", "Hydrogen-Ion Concentration", "Ion Channels", "Kinetics", "Potassium", "Rats", "Synaptosomes" ], "QualifierName": [ "", "drug effects", "metabolism", "metabolism", "", "", "drug effects", "", "pharmacology", "", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45400", "PMC1328524", "S0006-3495(79)85253-4", "10.1016/S0006-3495(79)85253-4" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 5, 5, 5 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45401, "DateCompleted": { "Year": 1981, "Month": 10, "Day": 25 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 6, "Day": 6 }, "Article": { "Abstract": { "AbstractText": "Lipid bilayer permeation coefficients for the neutral maleic acid molecule and the maleate monoanion have been determined by proton magnetic resonance techniques. Phosphatiydylcholine-cholesterol (2:1) unilamellar vesicles were prepared having an initial maleate anion concentration gradient stabilized by coupling to an impermeant potassium counterion. The coupling was released by addition of valinomycin, and the time evolution of external pH, internal pH, and maleate concentration followed using nuclear magnetic resonance areas and chemical shifts. Transport rate equations were numerically integrated to fit the date, yielding best fit permeation coefficients of 4 X 10(-9) and 4 X 10(-5) cm/s for maleate monoanion and maleic acid, respectively." }, "ArticleTitle": "Nuclear magnetic resonance determinations of permeation coefficients for maleic acid in phospholipid vesicles.", "AuthorList": { "Author": { "LastName": [ "Prestegard", "Cramer", "Viscio" ], "ForeName": [ "J H", "J A", "D B" ], "Initials": [ "JH", "JA", "DB" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "GM 19035", "RR 00798" ], "Agency": [ "NIGMS NIH HHS", "NCRR NIH HHS" ], "Country": [ "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "2001-95-8", "91XW058U2C", "97C5T2UQ7J" ], "NameOfSubstance": [ "Lipid Bilayers", "Maleates", "Phosphatidylcholines", "Valinomycin", "maleic acid", "Cholesterol" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Cholesterol", "Hydrogen-Ion Concentration", "Lipid Bilayers", "Magnetic Resonance Spectroscopy", "Maleates", "Mathematics", "Models, Biological", "Permeability", "Phosphatidylcholines", "Valinomycin" ], "QualifierName": [ "", "", "", "", "", "", "", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45401", "PMC1328571", "S0006-3495(79)85272-8", "10.1016/s0006-3495(79)85272-8" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 6, 6, 6 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45402, "DateCompleted": { "Year": 1981, "Month": 10, "Day": 25 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2018, "Month": 11, "Day": 13 }, "Article": { "Abstract": { "AbstractText": "The viscoelastic behavior of rat 9L cellular DNA was studied as a function of the detergent used for lysis, the pH and duration of lysis, and gamma ray dose. For nondenaturing lysis conditions, a model of the DNA was proposed to account for the effects of these agents on the viscoelastic retardation time. It was concluded that these agents affect the hydrodynamic radius of the DNA rather than its molecular weight. For denaturing lysis conditions, molecular weights calculated from the relaxation time were consistent with those calculated from alkaline sucrose sedimentation profiles." }, "ArticleTitle": "Viscoelastic behavior of mammalian DNA.", "AuthorList": { "Author": { "LastName": [ "Chase", "Shafer" ], "ForeName": [ "E S", "R H" ], "Initials": [ "ES", "RH" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "#5-TO1-GM-00829-14", "CA-13525", "CA19658" ], "Agency": [ "NIGMS NIH HHS", "NCI NIH HHS", "NCI NIH HHS" ], "Country": [ "United States", "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, Non-U.S. Gov't", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "9007-49-2" ], "NameOfSubstance": [ "DNA" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Animals", "Brain Neoplasms", "Cell Line", "DNA", "Elasticity", "Hydrogen-Ion Concentration", "Kinetics", "Neoplasms, Experimental", "Nucleic Acid Conformation", "Rats", "Viscosity" ], "QualifierName": [ "", "", "", "radiation effects", "", "", "", "", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45402", "PMC1328612", "S0006-3495(79)85161-9", "10.1016/S0006-3495(79)85161-9" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 10, 10, 10 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45411, "DateCompleted": { "Year": 1981, "Month": 11, "Day": 24 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2018, "Month": 11, "Day": 13 }, "Article": { "Abstract": { "AbstractText": "The Hodgkin-Huxley kinetic parameters, alpha h and beta h, which govern the rate of recovery from and development of sodium channel inactivation, respectively, have been measured as a function of membrane potential and external pH using a three-pulse protocol. alpha h but not beta h is substantially accelerated by reducing external pH from 7.4 to 6.4. The alpha h vs. voltage curve appears to be selectively shifted in the depolarizing direction by approximately 12 mV for this pH change, giving an apparent, h infinity curve shift of approximately 6 mV in the same direction (less inactivation)." }, "ArticleTitle": "Extracellular pH selectively modulates recovery from sodium inactivation in frog myelinated nerve.", "AuthorList": { "Author": { "LastName": [ "Courtney" ], "ForeName": [ "K R" ], "Initials": [ "KR" ], "CollectiveName": [ "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "HL24156-01" ], "Agency": [ "NHLBI NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "9NEZ333N27" ], "NameOfSubstance": [ "Sodium" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Animals", "Hydrogen-Ion Concentration", "Kinetics", "Models, Biological", "Myelin Sheath", "Rana catesbeiana", "Sciatic Nerve", "Sodium" ], "QualifierName": [ "", "", "", "", "drug effects", "", "drug effects", "pharmacology" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45411", "PMC1328637", "S0006-3495(79)85183-8", "10.1016/S0006-3495(79)85183-8" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 11, 11, 11 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45460, "DateCompleted": { "Year": 1983, "Month": 6, "Day": 17 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2018, "Month": 11, "Day": 30 }, "Article": { "Abstract": { "AbstractText": "Recent evidence suggests that of calcitonin (CT) and parathyroid hormone (PTH) is controlled by factors other than the ambient serum calcium concentration. We studied the effects of infusions of four neuroendocrine modulators upon CT and PTH levels: isoproterenol (beta-adrenergic agonist), methoxamine (alpha adrenergic agonist), prostaglandin E2, and somatostatin. Isoproterenol was a consistent secretagogue for both hormones. Maximal CT increments during isoproterenol infusion in normal subjects were 13 +/- 2 pg/ml (mean +/- SEM, n = 6, P less than 0.001; basal, 26 +/- 5). Maximal increments in PTH were 113 +/- 22 pg/ml (P less than 0.01, n = 6; basal, 430 +/- 11). Infusions of methoxamine increased CT by 13 +/- 5 pg/ml (n = 5, P less than 0.05; basal, 43 +/- 13), but had no effect on PTH. The means of the maximal CT increments during isoproterenol (21 +/- 8 pg/ml) and methoxamine infusion (28 +/- 11 pg/ml) were not statistically different from those achieved by acute elevations of serum calcium levels within the physiological range (41 +/- 23 pg/ml). Infusions of somatostatin and prostaglandin E2 had no or only transient effects on basal or stimulated CT or PTH levels. Our data suggest that adrenergic input modulates CT and PTH secretion in humans independently of changes in serum calcium." }, "ArticleTitle": "Neuroendocrine modulation of calcitonin and parathyroid hormone in man.", "AuthorList": { "Author": { "LastName": [ "Metz", "Deftos", "Baylink", "Robertson" ], "ForeName": [ "S A", "L J", "D J", "R P" ], "Initials": [ "SA", "LJ", "DJ", "RP" ], "CollectiveName": [ "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "AM-12829", "AM-15888", "HD-04872" ], "Agency": [ "NIADDK NIH HHS", "NIADDK NIH HHS", "NICHD NIH HHS" ], "Country": [ "United States", "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, Non-U.S. Gov't", "Research Support, U.S. Gov't, Non-P.H.S.", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "51110-01-1", "9007-12-9", "HUQ1KC1YLI", "K7Q1JQR04M", "L628TT009W", "SY7Q814VUP" ], "NameOfSubstance": [ "Parathyroid Hormone", "Prostaglandins E", "Somatostatin", "Calcitonin", "Methoxamine", "Dinoprostone", "Isoproterenol", "Calcium" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adult", "Calcitonin", "Calcium", "Dinoprostone", "Humans", "Isoproterenol", "Methoxamine", "Middle Aged", "Parathyroid Hormone", "Prostaglandins E", "Reference Values", "Somatostatin" ], "QualifierName": [ "", "blood", "blood", "", "", "", "", "", "blood", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45460", "10.1210/jcem-47-1-151" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 7, 7, 7 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45461, "DateCompleted": { "Year": 1983, "Month": 6, "Day": 17 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2018, "Month": 11, "Day": 30 }, "Article": { "Abstract": { "AbstractText": "In human placental explants cultured in vitro, dopamine inhibited human chorionic somatomammotropin (hCS) secretion into the culture media. In the control flasks, the level of hCS secretion was 130.5 +/- 7.8 micrograms/g tissue (n = 6). When 1 mM dopamine was added, hCS levels decreased to 80.2 +/- 11.5 micrograms/g tissue (P less than 0.01). Dopamine (5 and 10 mM) further lowered hCS levels. In contrast, 1 mM pimozide enhanced hCS secretion by 2-fold as compared to control levels (248.2 +/- 44.8 vs. 130.5 +/- 7.8, P less than 0.02). The simultaneous addition of dopamine did not alter the stimulatory effect of pimozide on hCS secretion. In separate experiments, arginine (1 and 5 mM) and somatostatin (1 microgram/ml culture media) did not alter hCS secretion from placental explants. These results suggest that hCS secretion is modulated by dopaminergic receptors." }, "ArticleTitle": "In vitro effect of dopamine and pimozide on human chorionic somatomammotropin (hCS) secretion.", "AuthorList": { "Author": { "LastName": [ "Macaron", "Famuyiwa", "Singh" ], "ForeName": [ "C", "O", "S P" ], "Initials": [ "C", "O", "SP" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "BR-5366" ], "Agency": [ "FDA HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "1HIZ4DL86F", "51110-01-1", "9035-54-5", "94ZLA3W45F", "IY9XDZ35W2", "VTD58H1Z2X" ], "NameOfSubstance": [ "Pimozide", "Somatostatin", "Placental Lactogen", "Arginine", "Glucose", "Dopamine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Arginine", "Dopamine", "Female", "Glucose", "Humans", "Kinetics", "Organ Culture Techniques", "Pimozide", "Placenta", "Placental Lactogen", "Pregnancy", "Somatostatin" ], "QualifierName": [ "pharmacology", "pharmacology", "", "metabolism", "", "", "", "pharmacology", "drug effects", "metabolism", "", "pharmacology" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45461", "10.1210/jcem-47-1-168" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 7, 7, 7 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45462, "DateCompleted": { "Year": 1983, "Month": 6, "Day": 17 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2007, "Month": 11, "Day": 14 }, "Article": { "Abstract": { "AbstractText": "The zoological specificity of human thyroid-stimulating antibody (TSAb) that occurs in the blood in Graves' disease was examined by assessing its effect on the thyroid of the dog, guinea pig, calf, and mouse as well as that of man. With all but murine glands, thyroid stimulation was assayed by measuring the increase in the concentration of cAMP in the thyroid slices or fragments after 2 h of incubation in buffer containing TSAb. Effects on the thyroid of the mouse were monitored by the in vivo bioassay for LATS. Sera from 33 patients with Graves' disease were obtained and concentrates of TSAb were prepared by precipitation of IgG with 1.64 M (NH4)2SO4. These all stimulated the human thyroid, 13 were LATS-positive, and they variably affected the tissues of other species; of 27 tested, 14 stimulated the thyroid of the dog, 8 out of 23 stimulated the thyroid of the guinea pig, and 12 out of 16 stimulated the gland of the calf. The more potent the TSAb as assayed with human tissue, the more likely was it to stimulate other species of thyroid; however, frequent exceptions occurred. In a separate analysis of 35 LATS-positive preparations of TSAb, correlation between the responses in the LATS and human thyroid slice assays was statistically significant (P less than 0.001). The data are compatible with the view that stimulation by TSAb of nonhuman thyroids, including the murine as in the LATS bioassay, reflects cross-reaction of this immunoglobulin with an antigen that has sufficient similarity to the human molecule to be recognized by the human antibody." }, "ArticleTitle": "Zoological specificity of human thyroid-stimulating antibody.", "AuthorList": { "Author": { "LastName": [ "Zakarija", "McKenzie" ], "ForeName": [ "M", "J M" ], "Initials": [ "M", "JM" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "AM-04121" ], "Agency": [ "NIADDK NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Comparative Study", "Journal Article", "Research Support, Non-U.S. Gov't", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "9002-71-5" ], "NameOfSubstance": [ "Antibodies", "Immunoglobulins, Thyroid-Stimulating", "Thyrotropin" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Animals", "Antibodies", "Cattle", "Dogs", "Graves Disease", "Guinea Pigs", "Humans", "Immunoglobulins, Thyroid-Stimulating", "Mice", "Reference Values", "Species Specificity", "Thyroid Gland", "Thyrotropin" ], "QualifierName": [ "", "analysis", "", "", "immunology", "", "", "", "", "", "", "drug effects", "pharmacology" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45462", "10.1210/jcem-47-2-249" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 8, 8, 8 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45464, "DateCompleted": { "Year": 1983, "Month": 6, "Day": 17 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2015, "Month": 11, "Day": 19 }, "Article": { "Abstract": { "AbstractText": "To determine if the adrenergic nervous system, and specifically tyrosine hydroxylase, plays a role in the extrathyroidal conversion of T4 to T3, normal male volunteers were treated with T4 and subsequently with T4 and alpha-methyl-p-tyrosine (alpha-MPT), an inhibitor of tyrosine hydroxylase, for 2 weeks. The mean serum T4 and T3 concentrations increased during T4 administration and remained at the same levels during combined T4 and alpha-MPT administration. Urinary vanillylmandelic acid excretion declined significantly during alpha-MPT administration. These results do not support the hypothesis that tyrosine hydroxylase is involved in extrathyroidal T3 production." }, "ArticleTitle": "Failure of alpha-methyltyrosine to inhibit peripheral triiodothyronine formation.", "AuthorList": { "Author": { "LastName": [ "Dvorak", "Engelman", "Utiger" ], "ForeName": [ "J C", "K", "R D" ], "Initials": [ "JC", "K", "RD" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "AM-14039", "RR-40" ], "Agency": [ "NIADDK NIH HHS", "NCRR NIH HHS" ], "Country": [ "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "06LU7C9H1V", "658-48-0", "EC 1.14.16.2", "Q51BO43MG4" ], "NameOfSubstance": [ "Methyltyrosines", "Triiodothyronine", "alpha-Methyltyrosine", "Tyrosine 3-Monooxygenase", "Thyroxine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adult", "Humans", "Kinetics", "Male", "Methyltyrosines", "Thyroxine", "Triiodothyronine", "Tyrosine 3-Monooxygenase", "alpha-Methyltyrosine" ], "QualifierName": [ "", "", "", "", "", "blood", "biosynthesis", "antagonists & inhibitors", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45464", "10.1210/jcem-47-2-442" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 8, 8, 8 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45468, "DateCompleted": { "Year": 1983, "Month": 6, "Day": 17 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2008, "Month": 11, "Day": 21 }, "Article": { "Abstract": { "AbstractText": "Normal human plasma contains \"inactive renin,\" whose ability to generate angiotensin I increases after exposure to pH 3.3. Big renin is a partially inactive enzyme of larger molecular weight, which is also activated at pH 3.3, and is found of pregnant women, and in amniotic fluid, but not in normal plasma. We have compared the effects of acid exposure and storage at 4 and -4 C on normal plasma and plasma containing big renin. The concentration of inactive renin in normal plasma was approximately equal to that of normal active renin, and its activity increased slowly on prolonged standing at -4 but not 4 C. In contrast, the activity of big renin increased by 50% as early as 1-3 days at 4 C and increased even more quickly at -4 C. Acid treatment of plasma containing big renin caused 4-10 times greater increase in active renin than similar treatment of normal plasma. During gel filtration, both cold-activated and previously acidified big renin coeluted with unactivated big renin. These data indicate that big renin is highly susceptible to cold or acid activation and that such activation of big renin does not result in a detectable decrease in its molecular weight of 60,000 daltons. Furthermore, acid and cold seem to activate the same pool of inactive renin in normal plasma. Although both normal and big renin are stable for long periods below -20 C, a serious overestimate of plasma renin activity can occur if plasma is stored just above its freezing point before assay." }, "ArticleTitle": "A comparison of cold and acid activation of big renin and of inactive renin in normal plasma.", "AuthorList": { "Author": { "LastName": [ "Hsueh", "Luetscher", "Carlson", "Grislis", "Elbaum", "Chavarri" ], "ForeName": [ "W A", "J A", "E", "G", "D", "M" ], "Initials": [ "WA", "JA", "E", "G", "D", "M" ], "CollectiveName": [ "", "", "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "HL-13917", "HL-17364", "RR-70" ], "Agency": [ "NHLBI NIH HHS", "NHLBI NIH HHS", "NCRR NIH HHS" ], "Country": [ "United States", "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Comparative Study", "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "EC 3.4.23.15" ], "NameOfSubstance": [ "Enzyme Precursors", "Renin" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Amniotic Fluid", "Chromatography, Gel", "Cold Temperature", "Diabetic Nephropathies", "Enzyme Activation", "Enzyme Precursors", "Female", "Humans", "Hydrogen-Ion Concentration", "Pregnancy", "Renin" ], "QualifierName": [ "enzymology", "", "", "blood", "", "blood", "", "", "", "", "blood" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45468", "10.1210/jcem-47-4-792" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 10, 10, 10 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45469, "DateCompleted": { "Year": 1983, "Month": 6, "Day": 17 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2018, "Month": 11, "Day": 30 }, "Article": { "Abstract": { "AbstractText": "Plasma PRL was measured at 20-min intervals in six patients with Parkinson's disease under various treatment protocols. In addition, 24-h mean GH levels were measured. The results of these studies showed that two untreated patients with Parkinson's disease had normal 24-h mean PRL levels with the normal increase during sleep. During chronic treatment with L-dopa-carbidopa (Sinemet), the 24-h PRL level was 12.8 +/- 4.9 ng/ml (mean +/- SD) and there was persistence of augmented PRL secretion during sleep. The 24-h mean GH level ranged from 1.5-4.4 ng/ml, with a mean of 2.5 ng/ml. The addition of a dopamine agonist (Lergotrile mesylate) resulted in a significant (P less than 0.01) suppression of the 24-h mean PRL levels and abolition of the normal sleep augmentation after 2 weeks of therapy. This suppression was maintained in one patient who was restudied 4 months after the addition of dopamine agonist therapy to L-dopa-carbidopa. The 24-h mean GH levels did not change significantly after the addition of the dopamine agonist when compared to L-dopa-carbidopa alone. These results suggest a dichotomy between the PRL and GH responses to combined L-dopa-carbidopa and dopamine agonist therapy. In addition, the preservation of normal PRL regulation in the two untreated patients with Parkinson's disease suggests that dopaminergic neurons are not universally affected in this disorder." }, "ArticleTitle": "Effect of dopamine agonist (Lergotrile mesylate) therapy on twenty-four hour secretion of prolactin in treated Parkinson's disease.", "AuthorList": { "Author": { "LastName": [ "Bell", "Carruth", "Rosenberg", "Boyar" ], "ForeName": [ "R D", "A", "R N", "R M" ], "Initials": [ "RD", "A", "RN", "RM" ], "CollectiveName": [ "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "1-K04 HD-00153", "5-M01-RR-00633", "HD-10909" ], "Agency": [ "NICHD NIH HHS", "NCRR NIH HHS", "NICHD NIH HHS" ], "Country": [ "United States", "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, Non-U.S. Gov't", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "46627O600J", "9002-62-4", "9002-72-6", "MNX7R8C5VO" ], "NameOfSubstance": [ "Drug Combinations", "Ergolines", "carbidopa, levodopa drug combination", "Levodopa", "Prolactin", "Growth Hormone", "Carbidopa" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adult", "Aged", "Carbidopa", "Circadian Rhythm", "Drug Combinations", "Drug Therapy, Combination", "Ergolines", "Female", "Growth Hormone", "Humans", "Levodopa", "Male", "Middle Aged", "Parkinson Disease", "Prolactin", "Sleep" ], "QualifierName": [ "", "", "therapeutic use", "drug effects", "therapeutic use", "", "therapeutic use", "", "metabolism", "", "therapeutic use", "", "", "drug therapy", "metabolism", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45469", "10.1210/jcem-47-4-807" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 10, 10, 10 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45471, "DateCompleted": { "Year": 1983, "Month": 6, "Day": 17 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2018, "Month": 11, "Day": 30 }, "Article": { "Abstract": { "AbstractText": "The effect of somatostatin (SRIF) on human chorionic somatomammotropin (hCS) secretion was studied in human placental explants cultured in vitro. In the experimental flasks, SRIF was added in a concentration of 10, 100, and 1000 ng/ml media; hCS levels measured by RIA were not different from those found in the control flasks. In separate experiments, we investigated the action of SRIF on hCG secretion by a human malignant choriocarcinoma cell line maintained in tissue culture. SRIF (1000 ng/ml) did not inhibit basal or dibutyryl cAMP-induced stimulation of hCG secretion. These results suggest that somatostatin does not suppress hCS or hCG release in vitro from normal or malignant trophoblast, respectively." }, "ArticleTitle": "Failure of somatostatin to affect human chorionic somatomammotropin and human chorionic gonadotropin secretion in vitro.", "AuthorList": { "Author": { "LastName": [ "Macaron", "Kyncl", "Rutsky", "Halpern", "Brewer" ], "ForeName": [ "C", "M", "L", "B", "J" ], "Initials": [ "C", "M", "L", "B", "J" ], "CollectiveName": [ "", "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "BR-5366" ], "Agency": [ "FDA HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "51110-01-1", "63X7MBT2LQ", "9035-54-5" ], "NameOfSubstance": [ "Chorionic Gonadotropin", "Somatostatin", "Bucladesine", "Placental Lactogen" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Bucladesine", "Cell Line", "Choriocarcinoma", "Chorionic Gonadotropin", "Female", "Humans", "Organ Culture Techniques", "Placenta", "Placental Lactogen", "Pregnancy", "Somatostatin", "Uterine Neoplasms" ], "QualifierName": [ "pharmacology", "", "metabolism", "metabolism", "", "", "", "drug effects", "metabolism", "", "pharmacology", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45471", "10.1210/jcem-47-5-1141" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 11, 11, 11 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45472, "DateCompleted": { "Year": 1983, "Month": 6, "Day": 17 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2015, "Month": 11, "Day": 19 }, "Article": { "Abstract": { "AbstractText": "The rise and subsequent return to basal of glucose production (Ra) during a constant glucagon infusion (\"downregulation\") has suggested to some workers that glucagon's effects are evanescent. To examine whether glucagon displays persistent biological activity even after downregulation, 6 healthy males received an 8 hour infusion of somatostatin and glucagon, with 3H-3-glucose to measure glucose turnover. Ra rose from 2.8 +/- 0.3 to 4.2 +/- 0.3 mg/kg . min at 90 minutes, returned to basal levels at 150 minutes, and remained at this level for the ensuing 330 minutes. Six additional subjects received an 8 hour somatostatin infusion, with glucagon administered concomitantly for the first 5 hours. Glucagon withdrawal at 5 hours produced an immediate decline in Ra from 1.8 +/- 0.2 to 0.9 +/- 0.2 mg/kg . min. Thus, even after downregulation the maintenance of basal Ra is dependent on circulating glucagon." }, "ArticleTitle": "Persistent stimulatory effect of glucagon on glucose production despite downregulation.", "AuthorList": { "Author": { "LastName": [ "Bloomgarden", "Liljenquist", "Cherrington", "Rabinowitz" ], "ForeName": [ "Z T", "J E", "A D", "D" ], "Initials": [ "ZT", "JE", "AD", "D" ], "CollectiveName": [ "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "1 R01 AM19587", "5 M01 RR-95" ], "Agency": [ "NIADDK NIH HHS", "NCRR NIH HHS" ], "Country": [ "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, Non-U.S. Gov't", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "51110-01-1", "9007-92-5", "IY9XDZ35W2" ], "NameOfSubstance": [ "Blood Glucose", "Insulin", "Somatostatin", "Glucagon", "Glucose" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adolescent", "Adult", "Blood Glucose", "Glucagon", "Glucose", "Humans", "Insulin", "Male", "Somatostatin" ], "QualifierName": [ "", "", "metabolism", "blood", "metabolism", "", "blood", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45472", "10.1210/jcem-47-5-1152" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 11, 11, 11 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45474, "DateCompleted": { "Year": 1983, "Month": 6, "Day": 17 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2007, "Month": 11, "Day": 14 }, "Article": { "Abstract": { "AbstractText": "We used a modification of the TSH radioreceptor assay to detect TSH-binding inhibition (TBI) activity in serum and serum fractions from normal subjects and patients with Graves' disease. TBI activity is present in normal IgG prepared by DEAE-Sephadex chromatography and in normal globulins prepared by precipitation at 1.6 M ammonium sulfate. Other normal serum proteins also had TBI activity when large concentrations were tested. Gel filtration chromatography and powder block electrophoresis were used to prepare fractions of normal and Graves' disease sera. In these fractions from normal serum. TBI activity was found in both gamma-globulin and alpha-globulin-albumin fractions electrophoretically and in both 7S and 4S peaks from gel filtration. TBI activity from Graves' disease patients' sera was similarly distributed, but relatively more TBI accompanied the electrophoretic gamma-globulins. Sepharose Protein-A and anti-IgG were used as immunoabsorbents to isolate and purify IgG from normal and Graves' disease sera. TBI activity in IgG was proportional to the IgG concentration, indicating that the TBI which migrates as a gamma-globulin electrophoretically is an IgG and thus may possibly be an antibody. Inhibitory activity found in normal serum globulins and the non-IgG fractions of both normal and abnormal sera seriously interferes with attempts to use the TSH radioreceptor assay to study the hypothesized anti-TSH, receptor antibody in the serum of patients with Graves' disease." }, "ArticleTitle": "Serum protein inhibition of thyrotropin binding to human thyroid tissue.", "AuthorList": { "Author": { "LastName": [ "Beall", "Chopra", "Solomon", "Kruger" ], "ForeName": [ "G N", "I J", "D H", "S R" ], "Initials": [ "GN", "IJ", "DH", "SR" ], "CollectiveName": [ "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "AM-17251", "AM-18316" ], "Agency": [ "NIADDK NIH HHS", "NIADDK NIH HHS" ], "Country": [ "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "9002-71-5" ], "NameOfSubstance": [ "Immunoglobulin G", "Immunoglobulins, Thyroid-Stimulating", "Thyrotropin" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Chromatography, Affinity", "Chromatography, Gel", "Electrophoresis", "Graves Disease", "Humans", "Immunoglobulin G", "Immunoglobulins, Thyroid-Stimulating", "Radioligand Assay", "Thyroid Gland", "Thyrotropin" ], "QualifierName": [ "", "", "", "immunology", "", "immunology", "", "", "metabolism", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45474", "10.1210/jcem-47-5-967" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 11, 11, 11 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45476, "DateCompleted": { "Year": 1983, "Month": 11, "Day": 23 }, "NumberOfReferences": 32, "DateRevised": { "Year": 2017, "Month": 11, "Day": 16 }, "Article": { "Abstract": { "AbstractText": "Intensive laboratory investigation of patients with recurrent infections, and with infections with microbial species not usually considered to be pathogenic, have led to the identification of several defects in granulocyte function. The two functions of granulocytes which have received most attention in the past decade have been locomotion (especially response to chemotactic stimulation) and microbicidal activity. Defective granulocyte chemotaxis has been demonstrated in patients with clinical manifestations suggesting abnormalities related to vasoactive amines, i.e., patients with eczema and extreme IgE hyperimmunoglobulinemia. The depressed granulocyte chemotactic responsiveness found in these patients can be reproduced in vitro when histamine and beta adrenergic agents are incubated with control granulocytes. Since these compounds have been shown to increase levels of intracellular cyclic AMP in other cells, there appears to be an association between cyclic nucleotide metabolism and regulation of granulocyte locomotion. Defective granulocyte microbicidal activity is found in patients with chronic granulomatous disease and it has been shown that there is little increase in oxidative metabolism during phagocytosis by these cells. Methods for quantitating the oxidative metabolism of granulocytes and monocytes include oxygen uptake, reduction of nitroblue tetrazolium, formate oxidation, and chemiluminescence response during phagocytosis. Since products of oxygen metabolism, i.e., hydrogen peroxide, superoxide or singlet oxygen do not accumulate in granulocyte phagocytic vacuoles, intracellular microbes are not killed (except bacterial species that produce hydrogen peroxide). The biochemical basis for defective oxidative metabolism in granulocytes from patients with chronic granulomatous disease appears to be associated with abnormal nucleotide oxidase activity." }, "ArticleTitle": "Disorders of phagocyte function: biochemical aspects.", "AuthorList": { "Author": { "LastName": [ "Quie" ], "ForeName": [ "P G" ], "Initials": [ "PG" ], "CollectiveName": [ "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "AI 06931", "AI 08821", "AI 12402" ], "Agency": [ "NIAID NIH HHS", "NIAID NIH HHS", "NIAID NIH HHS" ], "Country": [ "United States", "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S.", "Review" ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "53-59-8", "BBX060AN9V", "E0399OZS9N", "EC 1.11.1.7", "EC 1.6.-", "EC 1.6.3.-", "EC 3.-", "H2D2X058MU", "PHA4727WTP" ], "NameOfSubstance": [ "Nucleotides, Cyclic", "NADP", "Hydrogen Peroxide", "Cyclic AMP", "Peroxidase", "NADH, NADPH Oxidoreductases", "NADPH Oxidases", "Hydrolases", "Cyclic GMP", "Mannose" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Blood Bactericidal Activity", "Carbohydrate Metabolism, Inborn Errors", "Cell Movement", "Chediak-Higashi Syndrome", "Chemotaxis, Leukocyte", "Cyclic AMP", "Cyclic GMP", "Granulocytes", "Granulomatous Disease, Chronic", "Humans", "Hydrogen Peroxide", "Hydrogen-Ion Concentration", "Hydrolases", "Leukocytes", "Luminescent Measurements", "Mannose", "Metabolism, Inborn Errors", "NADH, NADPH Oxidoreductases", "NADP", "NADPH Oxidases", "Nucleotides, Cyclic", "Oxygen Consumption", "Peroxidase", "Phagocyte Bactericidal Dysfunction", "Phagocytosis", "Protein-Energy Malnutrition" ], "QualifierName": [ "", "blood", "", "blood", "", "blood", "blood", "enzymology", "blood", "", "metabolism", "", "blood", "physiology", "", "metabolism", "blood", "blood", "metabolism", "", "metabolism", "", "metabolism", "blood", "", "blood" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45476" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1977, 1977, 1977 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45478, "DateCompleted": { "Year": 1984, "Month": 5, "Day": 2 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2013, "Month": 11, "Day": 21 }, "Article": { "Abstract": { "AbstractText": "The clinical effectiveness of published algorithms in correcting serum total calcium (CaT) for the effects of protein, albumin, and pH was tested. Corrected calcium (CaC) values obtained by 13 of these methods were compared with values of measured free calcium (CaF) in 55 samples from normal controls and 404 samples from patients with various disorders of calcium metabolism. Three criteria were used to compare either CaC or CaT with measured CaF: 1) the correlation coefficient, 2) the average absolute deviation from measured CaF of the values of CaF predicted by the linear regression of CaF on each CaC, and 3) the number of samples in which CaC or CaT gave a different impression of normality than measured CaF. Application of the 13 published algorithms produced varied results, but none produced substantially better agreement between CaC and CaF than was found between CaT and CaF. The application of additional algorithms derived by multiple linear regression using our data base gave slightly better results than any of the published algorithms, but many values of CaC remained which were disparate from the measured value of CaF. Correction of measured total calcium by using other concurrently obtained chemistry values does not seem to adequately predict calcium status as measured by free calcium." }, "ArticleTitle": "Failure of total calcium corrected for protein, albumin, and pH to correctly assess free calcium status.", "AuthorList": { "Author": { "LastName": [ "Ladenson", "Lewis", "Boyd" ], "ForeName": [ "J H", "J W", "J C" ], "Initials": [ "JH", "JW", "JC" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "5-F32-6M05009-2" ], "Agency": [ "PHS HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "SY7Q814VUP" ], "NameOfSubstance": [ "Blood Proteins", "Serum Albumin", "Calcium" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Autoanalysis", "Blood Proteins", "Calcium", "Humans", "Hydrogen-Ion Concentration", "Hyperparathyroidism", "Protein Binding", "Reference Values", "Serum Albumin", "Spectrophotometry, Atomic" ], "QualifierName": [ "", "metabolism", "blood", "", "", "blood", "", "", "metabolism", "methods" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45478", "10.1210/jcem-46-6-986" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 6, 6, 6 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45481, "DateCompleted": { "Year": 1984, "Month": 11, "Day": 9 }, "NumberOfReferences": 58, "DateRevised": { "Year": 2019, "Month": 5, "Day": 9 }, "Article": { "Abstract": { "AbstractText": "Four characteristics of culture medium that are important to embryo development and nutrition of the blastocyst have been discussed. An examination of several of the most commonly used media for embryo culture demonstrates many similarities among them. The milliosmolarities of the media range from the hypoosmotic optimums (256 milliosmols) demonstrated in several in vitro studies to the physiologic range (308 to 315 milliosmols). Media between these extremes generally allow good development. Low oxygen concentrations (5%) in the culture environment allow somewhat better development of early cleavage stages, but recent studies suggest the difference between development in 5 and 20% oxygen to be less than originally thought. The media most commonly employed for early embryo culture contain bicarbonate as the buffer, but maintenance of pH is probably not the most crucial role of the CO2-bicarbonate content of the media. Likewise, since 1965 almost all media used to culture embryos have used pyruvate as the primary energy source. This is particularly important when early stages, before blastocyst development, are cultured. The concentration used generally falls within the optimum range of 2.5 to 5.0 X 10(-4)M first reported. Although glucose is not oxidized well by the early cleavage stages, it is an important energy source for all blastocysts. Furthermore, glucose contributes more than any other carbon source, including amino acids, to protein formation. Much is yet to be learned concerning the nutrition of the blastocyst, but our knowledge has increased immensely during the last 15 years. Hopefully our progress will be at least as rapid in the coming decade." }, "ArticleTitle": "Requirements for blastocyst development in vitro.", "AuthorList": { "Author": { "LastName": [ "Brinster", "Troike" ], "ForeName": [ "R L", "D E" ], "Initials": [ "RL", "DE" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "CA 14676", "HD 08539", "HD 12384" ], "Agency": [ "NCI NIH HHS", "NICHD NIH HHS", "NICHD NIH HHS" ], "Country": [ "United States", "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Comparative Study", "Journal Article", "Research Support, Non-U.S. Gov't", "Research Support, U.S. Gov't, P.H.S.", "Review" ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "142M471B3J", "8558G7RUTR", "IY9XDZ35W2", "S88TT14065" ], "NameOfSubstance": [ "Bicarbonates", "Culture Media", "Pyruvates", "Carbon Dioxide", "Pyruvic Acid", "Glucose", "Oxygen" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Animals", "Bicarbonates", "Blastocyst", "Carbon Dioxide", "Culture Media", "Glucose", "Growth", "Hydrogen-Ion Concentration", "In Vitro Techniques", "Mice", "Osmolar Concentration", "Oxygen", "Pyruvates", "Pyruvic Acid", "Rabbits" ], "QualifierName": [ "", "", "physiology", "metabolism", "", "metabolism", "", "", "", "", "", "", "metabolism", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45481", "10.1093/ansci/49.supplement_ii.26" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45485, "DateCompleted": { "Year": 1986, "Month": 6, "Day": 20 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2021, "Month": 5, "Day": 26 }, "Article": { "Abstract": { "AbstractText": "The kinetics of cell wall turnover in Bacillus subtilis have been examined in detail. After pulse labeling of the peptidoglycan with N-acetylglucosamine, the newly formed peptidoglycan is stable for approximately three-quarters of a generation and is then degraded by a process that follows first-order kinetics. Deprivation of an auxotroph of amino acids required for protein synthesis results in a cessation of turnover. If a period of amino acid starvation occurs during the lag phase of turnover, then the initiation of turnover is delayed for a period of time equivalent to the starvation period. During amino acid starvation, new cell wall peptidoglycan is synthesized and added to preexisting cell wall. This peptidoglycan after resumption of growth is also subject to degradation (turnover). It is suggested that cell wall turnover is dependent on cell growth and elongation. Several possible control mechanisms for cell wall autolytic enzymes are discussed in light of these observations." }, "ArticleTitle": "Relation between cell wall turnover and cell growth in Bacillus subtilis.", "AuthorList": { "Author": { "LastName": [ "Glaser", "Lindsay" ], "ForeName": [ "L", "B" ], "Initials": [ "L", "B" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "GM 18405" ], "Agency": [ "NIGMS NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "10028-17-8", "66974FR9Q1", "EC 3.5.1.28", "V956696549" ], "NameOfSubstance": [ "Amino Acids", "Carbon Radioisotopes", "Peptidoglycan", "Tritium", "Chloramphenicol", "N-Acetylmuramoyl-L-alanine Amidase", "Acetylglucosamine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Acetylglucosamine", "Amino Acids", "Bacillus subtilis", "Carbon Radioisotopes", "Cell Wall", "Chloramphenicol", "N-Acetylmuramoyl-L-alanine Amidase", "Peptidoglycan", "Tritium" ], "QualifierName": [ "metabolism", "metabolism", "growth & development", "", "metabolism", "pharmacology", "analysis", "metabolism", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45485", "PMC235259", "10.1128/jb.130.2.610-619.1977" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1977, 1977, 1977 ], "Month": [ 5, 5, 5 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45486, "DateCompleted": { "Year": 1986, "Month": 6, "Day": 20 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2021, "Month": 5, "Day": 26 }, "Article": { "Abstract": { "AbstractText": "Earlier studies indicated that the gene of an ammonium-inducible glutamate dehydrogenase (GDH) was inducible throughout the cell cycle and was expressible shortly after replication early in the S-phase in synchronous Chlorella cells growing at a rate of 13% per h in the absence of inducer. In the present study, synchronous cells cultured at the same growth rate in the continuous presence of inducer accumulated this enzyme in a linear manner, with a positive rate change observed late instead of early in the S-phase. At a growth rate of 26% per h, the positive rate change appeared to be displaced to 1.5 h before the S-phase in the next cell cycle. With 2'-deoxyadenosine, an in vivo inhibitor of deoxyribonucleic acid (DNA) synthesis, the magnitude of the positive rate change was shown to be proportional to the relative increase in DNA in the previous cell cycle. Collectively, these data support the idea that expression of newly replicated genes of this enzyme can be delayed into the subsequent cell cycle in cells in the continuous presence of inducer. Studies with cycloheximide indicated that the inducible GDH and another GDH isozyme were stable in fully induced cells in the absence of protein synthesis. However, after ammonium was removed from the culture medium, the activity of the inducible GDH decreased rapidly in vivo, with a half-time of 5 to 10 min at 38.5 degrees C, whereas the rate of accumulation of the other GDH isozyme did not change. Addition of cycloheximide, at the time of inducer removal, prevented this loss in activity of the inducible GDH. The inability to rescue the activity of the inducible GDH, by readdition of ammonium during the deinduction period, indicates that this enzyme probably underwent irreversible inactivation and/or proteolytic degradation." }, "ArticleTitle": "Regulation of accumulation and turnover of an inducible glutamate dehydrogenase in synchronous cultures of Chlorella.", "AuthorList": { "Author": { "LastName": [ "Israel", "Gronostajski", "Yeung", "Schmidt" ], "ForeName": [ "D W", "R M", "A T", "R R" ], "Initials": [ "DW", "RM", "AT", "RR" ], "CollectiveName": [ "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "GM 19871" ], "Agency": [ "NIGMS NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, Non-P.H.S.", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "53-59-8", "9007-49-2", "98600C0908", "EC 1.4.1.2" ], "NameOfSubstance": [ "Culture Media", "Isoenzymes", "Nitrates", "NADP", "DNA", "Cycloheximide", "Glutamate Dehydrogenase" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Chlorella", "Culture Media", "Cycloheximide", "DNA", "DNA Replication", "Enzyme Induction", "Glutamate Dehydrogenase", "Interphase", "Isoenzymes", "Kinetics", "NADP", "Nitrates" ], "QualifierName": [ "enzymology", "", "pharmacology", "biosynthesis", "", "", "metabolism", "", "metabolism", "", "pharmacology", "pharmacology" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45486", "PMC235283", "10.1128/jb.130.2.793-804.1977" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1977, 1977, 1977 ], "Month": [ 5, 5, 5 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45487, "DateCompleted": { "Year": 1986, "Month": 6, "Day": 20 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2021, "Month": 5, "Day": 26 }, "Article": { "Abstract": { "AbstractText": "The effect of different extraction procedures on the yields of water-soluble and water-insoluble glycogen fractions from a number of Saccharomyces strains was studied by using a specific method for glycogen determination. The similarity of the yields obtained by the different procedures showed that neither form of glycogen is an artifact, and variations in the relative amounts of glycogen in the two fractions during cell growth and in different yeast strains suggest that they represent different pools of storage material with specific roles in cell development and differentiation. A proportion of the water-insoluble glycogen fraction, solubilized by mechanical agitation, was shown to be strongly associated with a beta-glucan-like polysaccharide that may be a cell wall component." }, "ArticleTitle": "Two pools of glycogen in Saccharomyces.", "AuthorList": { "Author": { "LastName": [ "Gunja-Smith", "Patil", "Smith" ], "ForeName": [ "Z", "N B", "E E" ], "Initials": [ "Z", "NB", "EE" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "AM 12532" ], "Agency": [ "NIADDK NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "9005-79-2" ], "NameOfSubstance": [ "Polysaccharides", "Glycogen" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Cell Wall", "Glycogen", "Hydrogen-Ion Concentration", "Polysaccharides", "Saccharomyces", "Solubility" ], "QualifierName": [ "metabolism", "analysis", "", "analysis", "analysis", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45487", "PMC235286", "10.1128/jb.130.2.818-825.1977" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1977, 1977, 1977 ], "Month": [ 5, 5, 5 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45488, "DateCompleted": { "Year": 1986, "Month": 6, "Day": 20 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2021, "Month": 5, "Day": 26 }, "Article": { "Abstract": { "AbstractText": "Enzymatic methyl ester formation in Escherichia coli ribosomal proteins was observed. Alkali lability of the methylated proteins and derivatization of the methyl groups as methyl esters of 3,5-dinitrobenzoate indicate the presence of protein methyl esters. The esterification reaction occurs predominantly on the 30S ribosomal subunit, with protein S3 as the major esterified protein. When the purified 30S subunit was used as the methyl acceptor, protein S9 was also found to be esterified. The enzyme responsible for the esterification of free carboxyl groups in proteins, protein methylase II (S-adenosyl-L-methionine:protein carboxyl methyltransferase, EC 2.1.1.24), was identified in E. coli Q13. This enzyme is extremely unstable when compared with that from mammalian origin. By molecular sieve chromatography, E. coli protein methylase II showed multiple peaks, with a major broad peak around 120,000 daltons and several minor peaks in the lower-molecular-weight region. Rechromatography of the major enzyme peak showed activities in several fractions that are much lower in molecular weight. The substrate specificity of the E. coli enzyme is similar to that of the mammalian enzyme. The Km value for S-adenosyl-L-methionine is 1.96 X 10(-6) M, and S-adenosyl-L-homocysteine was found to be a competitive inhibitor, with a Ki value of 1.75 X 10(-6) M." }, "ArticleTitle": "Enzymatic methyl esterification of Escherichia coli ribosomal proteins.", "AuthorList": { "Author": { "LastName": [ "Kim", "Lew", "Chang" ], "ForeName": [ "S", "B", "F N" ], "Initials": [ "S", "B", "FN" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "GM 19302", "GM 20594" ], "Agency": [ "NIGMS NIH HHS", "NIGMS NIH HHS" ], "Country": [ "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "EC 2.1.1.-", "EC 2.1.1.-", "Y4S76JWI15" ], "NameOfSubstance": [ "Ribosomal Proteins", "Protein Methyltransferases", "Protein O-Methyltransferase", "Methanol" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Chromatography, Gel", "Escherichia coli", "Esterification", "Hydrogen-Ion Concentration", "Methanol", "Methylation", "Protein Methyltransferases", "Protein O-Methyltransferase", "Ribosomal Proteins" ], "QualifierName": [ "", "enzymology", "", "", "metabolism", "", "analysis", "analysis", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45488", "PMC235289", "10.1128/jb.130.2.839-845.1977" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1977, 1977, 1977 ], "Month": [ 5, 5, 5 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45497, "DateCompleted": { "Year": 1987, "Month": 1, "Day": 5 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2007, "Month": 11, "Day": 14 }, "Article": { "Abstract": { "AbstractText": "Preservation of donor tissue for human keratoplasty has been evaluated using modified M-K medium. The medium has been modified by changing the antibiotic and buffer and adding a pH indicator. These changes offered theoretical and practical advantages. There were no primary donor failures in 50 consecutive penetrating keratoplasties with an overall success rate of 92 percent. Clinical specular microscopy revealed good endothelial cell survival." }, "ArticleTitle": "Human penetrating keratoplasty using modified M-K medium.", "AuthorList": { "Author": { "LastName": [ "Waltman", "Palmberg" ], "ForeName": [ "S R", "P F" ], "Initials": [ "SR", "PF" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "EY-01167" ], "Agency": [ "NEI NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0" ], "NameOfSubstance": [ "Culture Media" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Corneal Transplantation", "Culture Media", "Endothelium", "Humans", "Hydrogen-Ion Concentration", "Preservation, Biological" ], "QualifierName": [ "", "", "", "", "", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45497" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 4, 4, 4 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45500, "DateCompleted": { "Year": 1987, "Month": 4, "Day": 23 }, "NumberOfReferences": 45, "DateRevised": { "Year": 2019, "Month": 8, "Day": 16 }, "Article": { "Abstract": { "AbstractText": "The various neurohumoral and intrinsic factors that control the uteroplacental hemodynamics in health and disease and in responses to physiologic and pharmacologic stimuli have been reviewed. The following conclusions may be derived: We still need improvement in our methodology of monitoring uterine blood flow. The present methods, which have some reliability, are not easily applicable to human subjects and even in animals their use presents problems of accuracy and sensitivity with which the investigator must become familiar. The marked and progressive increase in uterine blood flow that occurs during pregnancy is caused by complex factors, some of which are hormonal and hemodynamic in nature. The increased vascularity of the pregnant uterus and the opening of the arterioles during the process of formation of the intervillous space are important factors that facilitate the increase in uterine blood flow. The increment seems to be totally derived from the increment in the cardiac output that occurs during pregnancy. There seems to be no redistribution among the regional blood flows of the body. In the anesthetized condition the blood flow to the uterus depends largely on the perfusing pressure; the critical closing pressure seems to be around the 40 mm Hg level. This linear flow-pressure relationship does not, however, apply to the unanesthetized condition. A rise or fall in the perfusing pressure in the conscious state may be accompanied by an increase or decrease in the uterine blood flow, depending on the underlying mechanisms. Factors that lead to alpha-adrenergic stimulation produce an increase in uterine vascular resistance and a decrease in flow, irrespective of the status of the perfusing pressure. beta-adrenergic stimulation may increase uterine blood flow either through their vasodilating action or through their myometrial relaxing effects. Hypertensive diseases are most often accompanied by a decrease in uterine blood flow, whereas hypoxic states may decrease the flow even though the arterial pressure may not change significantly. It is extremely risky to extrapolate from information obtained in the anesthetized animal to the unanesthetized, conscious animal. Likewise, data obtained from normotensive conditions may not hold true for the hypertensive or hypotensive states. This is of particular relevance when one is dealing with the effects of pharmacologic agents that act on the cardiovascular system. Uterine contractions, whether induced through spontaneous or oxytocin-induced labor, produce a decrease in uterine blood flow.(ABSTRACT TRUNCATED AT 400 WORDS)" }, "ArticleTitle": "Control of the uteroplacental circulation in health and disease.", "AuthorList": { "Author": { "LastName": [ "Asśali", "Nuwayhid", "Zugaib" ], "ForeName": [ "N S", "B", "M" ], "Initials": [ "NS", "B", "M" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "HL-01755" ], "Agency": [ "NHLBI NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S.", "Review" ] } }, "MedlineJournalInfo": { "Country": "Ireland" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0" ], "NameOfSubstance": [ "Adrenergic beta-Agonists", "Anesthetics", "Hormones" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adrenergic beta-Agonists", "Anesthetics", "Animals", "Female", "Hemodynamics", "Hormones", "Humans", "Labor, Obstetric", "Placenta", "Pregnancy", "Pregnancy Complications", "Regional Blood Flow", "Uterus" ], "QualifierName": [ "pharmacology", "pharmacology", "", "", "drug effects", "pharmacology", "", "physiology", "blood supply", "physiology", "physiopathology", "drug effects", "blood supply" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45500", "0028-2243(78)90008-4", "10.1016/0028-2243(78)90008-4" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1978, 1978, 1978 ], "Month": [ 2, 2, 2 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45498, "DateCompleted": { "Year": 1986, "Month": 12, "Day": 31 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 12, "Day": 10 }, "Article": { "Abstract": { "AbstractText": "The reinforcing properties of etonitazene, both conditioned and unconditioned, were measured in rats that had received saline only by continuous intravenous infusion (\"saline\" group) and in two groups of rats that had been physically dependent on morphine to equal degrees (and presumably had developed equal degrees of tolerance to morphine): one by once daily passive intravenous injection of morphine (\"injection\" group) and the other by passive continuous intravenous morphine infusion at the same daily doses for approximately the same number of days (\"infusion\" group). Prior to passive saline and morphine administration, all rats were trained to press right- and left-sided levers for water reinforcement from 1600 to 0800 hrs to a not more than 60-40 split, and these and other measures (\"baselines\") were repeated after recovery from the early (acute) morphine-abstinence syndromes. Then etonitazene, 5 micrograms/ml, was substituted for water on the nonpreferred side and all measures were repeated from 1600 to 0800 hrs once every two weeks for 20 weeks (10 \"relapse\" tests). It was postulated that the daily cycles of morphine-abstinence and suppression of abstinence in the injection group only would generate latent interoceptively conditioned reinforcing properties of morphine because of conditioning of suppression of abstinence to the concomitant internal sensorial effects of morphine, which would persist after morphine withdrawal and be transferred to the internal effects of another opioid, etonitazene. It was found that across the first nine relapse tests, the injection group consumed significantly more etonitazene than the infusion group, while there were no significant differences in water consumption.(ABSTRACT TRUNCATED AT 250 WORDS)" }, "ArticleTitle": "Interoceptive conditioning through repeated suppression of morphine-abstinence. II. Relapse-testing.", "AuthorList": { "Author": { "LastName": [ "Miller", "Dougherty", "Wikler" ], "ForeName": [ "D B", "J A", "A" ], "Initials": [ "DB", "JA", "A" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "DA-01131" ], "Agency": [ "NIDA NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, Non-P.H.S.", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "76I7G6D29C" ], "NameOfSubstance": [ "Benzimidazoles", "Morphine" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Animals", "Benzimidazoles", "Conditioning, Classical", "Drinking", "Male", "Morphine", "Morphine Dependence", "Rats", "Rats, Inbred Lew", "Rats, Inbred Strains", "Reaction Time", "Recurrence", "Reinforcement, Psychology", "Self Administration", "Substance Withdrawal Syndrome" ], "QualifierName": [ "", "", "physiology", "", "", "adverse effects", "physiopathology", "", "", "", "physiology", "", "", "", "physiopathology" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45498", "10.1007/BF03001978" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 7, 7, 7 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45522, "DateCompleted": { "Year": 1989, "Month": 4, "Day": 12 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 8, "Day": 27 }, "Article": { "Abstract": { "AbstractText": "Emergence of antibiotic resistance is related to the ease of mutation, to the extent of exchange of genetic information in bacteria by conjugation, transformation, and transduction, and to the large-scale use of antimicrobial agents in the biosphere. In addition to the development of resistance through chromosomal mutation and exchange of chromosomal genes among organisms, there is a more profound enlargement of the gene pool by the dissemination and amplification of plasmids. Two examples of the exchange of antibiotic resistance are analyzed: the transfer of plasmids from Bacteroides fragilis to Escherichia coli and the emergence of antibiotic-resistant strains of STreptococcus pneumoniae. Plasmids encoding antibiotic resistance in B. fragilis were transferred to E. coli by DNA-mediated transformation and conjugation. The beta-lactamase in the transformants and transconjugants displayed the same substrate specificity and electrophoretic mobility as the donor strain. The plasmid apparently was integrated rapidly into the chromosome of the recipient strain. Multiple antibiotic-resistant strains of S. pneumoniae were analyzed for plasmids, and none were detected. Furthermore, no evidence of linkage between the traits of multiple antibiotic resistance was observed. beta-Lactamase was not detected in the penicillin-resistant strains; therefore, it is likely that the resistance in these strains was chromosomal rather than plasmid-mediated. The range of genetic exchange and the use of Koch's postulates in determining the genetic mechanism of antibiotic resistance are illustrated and discussed." }, "ArticleTitle": "Genetic determinants of microbial resistance to antibiotics.", "AuthorList": { "Author": { "LastName": [ "Young", "Mayer" ], "ForeName": [ "F E", "L" ], "Initials": [ "FE", "L" ], "CollectiveName": [ "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "AI-11709" ], "Agency": [ "NIAID NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "United States" }, "ChemicalList": { "Chemical": { "RegistryNumber": [], "NameOfSubstance": [] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Bacteria", "Bacteroides fragilis", "Conjugation, Genetic", "Drug Resistance, Microbial", "Escherichia coli", "R Factors", "Streptococcus pneumoniae", "Transformation, Bacterial" ], "QualifierName": [ "drug effects", "drug effects", "", "genetics", "drug effects", "", "drug effects", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45522", "10.1093/clinids/1.1.55" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45526, "DateCompleted": { "Year": 1989, "Month": 7, "Day": 5 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 8, "Day": 16 }, "Article": { "Abstract": { "AbstractText": "1. After separation by SDS gel-chromatography, analysis of AEP-containing glycoproteins from M. senile, indicated 66% amino acids with 220 AEP res./1000 res. and 30% carbohydrate for high mol. wt (greater than 10(7) forms and 80% amino acids with 25-50 AEP res./1000 res. and 10% carbohydrate for low mol. wt (2-4 x 10(4) forms. 2. Uronic acids, sulfate, lipid, and sialic acids were absent. 3. Mild base digestion released AEP-hexosamine containing oligosaccharides and destroyed ser-thr residues in the high mol. wt components. 4. Phosphonoglycoproteins appear to be acidic connective tissue components with AEP linked to hexosamine containing oligosaccharide side chains." }, "ArticleTitle": "Phosphonoglycoprotein from Metridium senile--heterogeneity of glycoproteins containing aminoethylphosphonic acid.", "AuthorList": { "Author": { "LastName": [ "Hurley", "Bunde", "Dell", "Kirkpatrick", "Bishop" ], "ForeName": [ "J C", "T A", "J C", "D S", "S H" ], "Initials": [ "JC", "TA", "JC", "DS", "SH" ], "CollectiveName": [ "", "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "AM-17372" ], "Agency": [ "NIADDK NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, Non-U.S. Gov't", "Research Support, U.S. Gov't, Non-P.H.S.", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "0", "AH00YJQ334" ], "NameOfSubstance": [ "Amino Acids", "Glycoproteins", "Organophosphorus Compounds", "Aminoethylphosphonic Acid" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Amino Acids", "Aminoethylphosphonic Acid", "Animals", "Chromatography, Gel", "Cnidaria", "Glycoproteins", "Hydrolysis", "Organophosphorus Compounds", "Sea Anemones" ], "QualifierName": [ "analysis", "metabolism", "", "", "metabolism", "isolation & purification", "", "metabolism", "metabolism" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45526", "10.1016/0305-0491(77)90199-7" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1977, 1977, 1977 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45529, "DateCompleted": { "Year": 1989, "Month": 7, "Day": 5 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 8, "Day": 16 }, "Article": { "Abstract": { "AbstractText": "1. The adenosine deaminase has an approximate molecular weight of 130,000-140,000 and the composition of two polypeptide units (mol. wt about 68,000) is suggested, by means of SDS disc electrophoresis. 2. Both the alpha (Vm/Km) and beta (Vm) parameters were varied with pH and temperature. RSS (relative substrate specificity) adenosine and deoxyadenosine values for alpha and beta were 1.2 and 1.1, respectively. 3. Adenine, 2'-, 3', 5'-AMP, 5'-deoxyAMP, ADP and ATP were not deaminated by the enzyme. 4. Inhibition by Mg2+ was found in reaction with adenosine at pH 8 but not with deoxyadenosine at the same pH. Mn2+, which did not affect the reaction rate at pH 4 and 5, showed competitive inhibitory effects at pH 6, 7 and 8." }, "ArticleTitle": "Purification and properties of the adenosine deaminase from the midgut gland of a marine bivalved mollusc, Atrina spp.", "AuthorList": { "Author": { "LastName": [ "Aikawa", "Umemori-Aikawa", "Fisher" ], "ForeName": [ "T", "Y", "J R" ], "Initials": [ "T", "Y", "JR" ], "CollectiveName": [ "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "GM-17506" ], "Agency": [ "NIGMS NIH HHS" ], "Country": [ "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, U.S. Gov't, Non-P.H.S.", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "42Z2K6ZL8P", "EC 3.5.4.-", "EC 3.5.4.4", "I38ZP9992A" ], "NameOfSubstance": [ "Manganese", "Nucleoside Deaminases", "Adenosine Deaminase", "Magnesium" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "Adenosine Deaminase", "Animals", "Chromatography, Gel", "Hydrogen-Ion Concentration", "Kinetics", "Magnesium", "Manganese", "Mollusca", "Nucleoside Deaminases", "Temperature" ], "QualifierName": [ "isolation & purification", "", "", "", "", "pharmacology", "pharmacology", "enzymology", "isolation & purification", "" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45529", "10.1016/0305-0491(77)90182-1" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1977, 1977, 1977 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }
{ "PMID": 45533, "DateCompleted": { "Year": 1989, "Month": 7, "Day": 13 }, "NumberOfReferences": 0, "DateRevised": { "Year": 2019, "Month": 8, "Day": 16 }, "Article": { "Abstract": { "AbstractText": "1. 2,4-Dinitrophenol (2,4-DNP) in substrate level concentrations (200 microM-1 mM) temporarily inhibits H2 production by Tritrichomonas foetus and Trichomonas vaginalis as well as the accumulation of metronidazole, dependent on its reduction by the two trichomonad species and by Entamoeba invadens. 2. 2,4-DNP competes for the reducing equivalents which are necessary for H2 production or for the reduction of metronidazole, thereby inhibiting these processes. 2,4-DNP is reduced to 2-amino, 4-nitrophenol. 3. 2,4-DNP in concentrations up to 800 microM has no effect on the uptake of O2 by these organisms. 4. 2,4-DNP has some toxicity for T. foetus." }, "ArticleTitle": "Effects of 2,4-dinitrophenol on trichomonads and Entamoeba invadens.", "AuthorList": { "Author": { "LastName": [ "Müller", "Nseka", "Mack", "Lindmark" ], "ForeName": [ "M", "V", "S R", "D G" ], "Initials": [ "M", "V", "SR", "DG" ], "CollectiveName": [ "", "", "", "" ] } }, "Language": "eng", "GrantList": { "Grant": { "GrantID": [ "AI11942", "AI12932" ], "Agency": [ "NIAID NIH HHS", "NIAID NIH HHS" ], "Country": [ "United States", "United States" ] } }, "PublicationTypeList": { "PublicationType": [ "Journal Article", "Research Support, Non-U.S. Gov't", "Research Support, U.S. Gov't, Non-P.H.S.", "Research Support, U.S. Gov't, P.H.S." ] } }, "MedlineJournalInfo": { "Country": "England" }, "ChemicalList": { "Chemical": { "RegistryNumber": [ "0", "0", "140QMO216E", "Q13SKS21MN" ], "NameOfSubstance": [ "Dinitrophenols", "Gases", "Metronidazole", "2,4-Dinitrophenol" ] } }, "CitationSubset": "IM", "MeshHeadingList": { "MeshHeading": { "DescriptorName": [ "2,4-Dinitrophenol", "Anaerobiosis", "Animals", "Color", "Dinitrophenols", "Entamoeba", "Gases", "Hydrogen-Ion Concentration", "Metronidazole", "Trichomonas", "Trichomonas vaginalis" ], "QualifierName": [ "", "", "", "", "pharmacology", "drug effects", "metabolism", "", "pharmacology", "drug effects", "drug effects" ] } } }
{ "ArticleIdList": { "ArticleId": [ [], [ "45533", "10.1016/0305-0491(79)90189-5" ] ] }, "PublicationStatus": "ppublish", "History": { "PubMedPubDate": { "Year": [ 1979, 1979, 1979 ], "Month": [ 1, 1, 1 ], "Day": [ 1, 1, 1 ] } }, "ReferenceList": { "Citation": [], "CitationId": [] } }

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