bluuebunny/crossref_metadata_2025_split huggingface dataset:
Rat hypothalamic extract inhibits vasopressin‐stimulated Na+‐K+‐ATPase activity in the rat renal medulla
Authors: Pippard Corinna , Baylis P. H. 
Published: May 2005

AbstractArginine vasopressin stimulates Na+‐K+‐ATPase activity located in the rat thick ascending limb of s'Henle loop. Mammalian hypothalamus appears to produce a factor capable of inhibiting Na+‐K+‐ATPase activity in a variety of tissues. The effect of a purified rat hypothalamic extract with and without AVP on rat renal Na+‐K+‐ATPase activity was evaluated by a cytochemical technique. The hypothalamic extract alone failed to affect basal Na+‐K+‐ATPase activity throughout renal segments after 10 min exposure. Na+‐K+‐ATPase activity stimulated by AVP (1–10 fmol l−1) for 10 min was inhibited by rat hypothalamic extract over the concentration range 10−7–10−3 U ml−1 in a dose‐dependent manner. Complete inhibition of AVP‐stimulated Na+‐K+‐ATPase activity occurred at a hypothalamic extract concentration of 10−3 U ml−1. Only Na+‐K+‐ATPase activity located in the renal medullary thick ascending limb was influenced by the rat hypothalamic extract.
A polyclonal antiserum against the rabbit progesterone receptor recognizes the human receptor: Biochemical characterization
Authors: Feil Peter D. , Clarke Christine L. , Satyaswaroop Pondichery G. 
Published: May 2005

AbstractPolyclonal antiserum was generated in guinea pigs immunized with the 116 000 Mr rabbit uterine progesterone receptor (PR). The PR antigen was partially purified by DEAE‐cellulose chromatography and preparative sodium dodecyl sulphate–polyacrylamide gel electrophoresis, transferred to nitrocellulose, and the 116 000 Mr band excised and injected into guinea pigs. The antiserum recognized on protein blots rabbit uterine PR of Mr 116 000 and 81 000. The antiserum was judged to be specific for PR from normal and malignant human tissues as determined by sedimentation shift on sucrose gradients, immunoprecipitation studies, protein blotting, and fluorographic analysis using photolabelled samples. Comparison of protein blots probed with this polyclonal antiserum or with a recently obtained monoclonal antibody to human PR indicated that similar PR structures were recognized in rabbit and human samples by both antisera. Characterization of the polyclonal antiserum has demonstrated its suitability for investigating the immunolocalization or PR in normal and malignant human tissues as well as the receptor structure detected on protein blots.
Chromatin organization in rat testis nuclei. Flow cytometric detection of the morphological compaction
Authors: Papa S. , Vitale M. , Rizzoli N. , Zini N. , Matteucci A. , Cecchini T. , Maraldi N. M. 
Published: May 2005

AbstractThe unusual histone composition of testicular cells generates changes in chromatin organization in order to allow the chromosomal pairing necessary for genetic recombination. Accessibility of testis nuclear DNA was determined by flow cytometry. The observed differences in staining between testis and liver nuclear chrmatin, as well as the differences of perpendicular light scatter signal, correlated with alterations in protein composition with the chromatin reorganization.
Susceptibility of Gamma‐Irradiated Proteins to In Vitro Glycation: Exposure to Oxygen Free Radicals Increases Glycation‐Induced Modifications
Authors: Traverso Nicola , Odetti Patrizio , Cheeseman Kevin , Cottalasso Damiano , Marinari Umberto Maria , Pronzato Maria Adelaide 
Published: May 2005

AbstractOxidation and glycation are non‐enzymatic protein modifications involved in the pathogenesis of aging. We evaluated their possible influences in an in vitro system: albumin was oxidized by gamma‐irradiation and then exposed to glycation in vitro. Fluorescence modifications were analysed as signals of protein alterations. Both radiolytic oxidation and in vitro glycation provoked a sharp decrease of tryptophan fluorescence (278 nm ex./340 nm em.); their effects tended to be additive, unless a saturation limit was reached. Both individually and in combination, these two non‐enzymatic processes induced the appearance of a new fluorescence (335 nm ex./415 nm em.); in this case as well there was an additive effect, with a trend toward saturation. Radiolytic oxidation and in vitro glycation seem to provoke similar damage to the exposed proteins: the observed fluorescence alterations may be due to similar conformational changes, breaks or the development of fluorophores.
The Taguchi influence on designed experiments
Authors: Stone R. A. , Veevers A. 
Published: May 2005

AbstractThis paper is intended to convey the essence of Taguchi's design approach to chemists and others with an interest in chemometrics. Although most Taguchi‐style applications worldwide have been in electronics and in elaborately transformed manufactures, examples are increasingly found in chemical processes and in the food industry.Foremost among Taguchi's contributions is the concept of designing processes and products to be robust to the uncontrollable environmental influences which they experience during their operation or lifetime. This concept is explained with a worked example.
ZnII–Salphen Complexes as Versatile Building Blocks for the Construction of Supramolecular Box Assemblies
Authors: Kleij Arjan W. , Kuil M. , Tooke Duncan M. , Lutz Martin , Spek Anthony L. , Reek Joost N. H. 
Published: May 2005

AbstractZnII–salphen complexes are readily accessible and interesting supramolecular building blocks with a large structural diversity. Higher‐order supramolecular assemblies, such as molecular boxes based on a bis‐ZnII–salphen building block and various ditopic bipyridine ligands, have been constructed by means of supramolecular, coordinative ZnII–Npyr interactions. The use of bipyridine ligands of differing sizes enables the construction of structures with predefined box diameters. The features of the 2:2 box assemblies were investigated in detail by (variable temperature) NMR spectroscopy, UV‐visible spectroscopy, NMR titrations, and X‐ray crystallographic studies. The spectroscopic studies reveal a high association constant for the ZnII–salphen–pyridyl motif, which lies in the range 105–106 M−1. The strong interaction between the ZnII center and pyridine donors was supported by PM3 calculations that showed a relatively high Lewis acid character of the metal center in the salphen complex. Titration curves monitored by UV‐visible show a cooperative effect between the two bipyridine ligands upon complexation to the bis‐ZnII template, suggesting the formation of 2:2 complexes. The crystal structures of two supramolecular boxes have been determined. In both examples such a 2:2 assembly is present in the solid state, and the box size is different because they consist of different building blocks. Interestingly, the box assemblies line up in the solid state to form porous channels that are potentially useful in a number of applications.
Synthesis and Crystal Structure of Bis(tetraethylammonium) Octabromo‐triselenate(II)‐{dibromodiselenate(I)}, [NEt4]2 [Se3Br8(Se2Br2)], the Salt of a Mixed‐Valence Bromoselenate(II,I) Anion.
Authors: Janickis Vitalijus , Milius Wolfgang , Toernroos Karl Wilhelm 
Published: May 2005

AbstractFor Abstract see ChemInform Abstract in Full Text.
The Satellite‐Shaped Co‐15 Polyoxotungstate, [Co6(H2O)30{Co9Cl2 (OH)3(H2O)9 (β‐SiW8O31)3}]5‐.
Authors: Bassil Bassem S. , Nellutla Saritha , Kortz Ulrich , Stowe Ashley C. , van Tol Johan , Dalal Naresh S. , Keita Bineta , Nadjo Louis 
Published: May 2005

AbstractFor Abstract see ChemInform Abstract in Full Text.
Diastereoselective Addition of Organolithiums to 1,3‐Oxazolidines Complexed with Aluminum Tris(2,6‐diphenylphenoxide) (ATPH).
Authors: Yamauchi Takayasu , Sazanami Hiroyuki , Sasaki Yuuichi , Higashiyama Kimio 
Published: May 2005

AbstractFor Abstract see ChemInform Abstract in Full Text.
Unusual and Unexpected Reactivity of t‐Butyl Dicarbonate (Boc2O) with Alcohols in the Presence of Magnesium Perchlorate. A New and General Route to t‐Butyl Ethers.
Authors: Bartoli Giuseppe , Bosco Marcella , Locatelli Manuela , Marcantoni Enrico , Melchiorre Paolo , Sambri Letizia 
Published: May 2005

AbstractFor Abstract see ChemInform Abstract in Full Text.
Five‐Membered 2,3‐Dioxo Heterocycles. Part 49. Reaction of Methyl 1‐Aryl‐3‐aroyl‐4,5‐dioxo‐4,5‐dihydro‐1H‐pyrrole‐2‐carboxylates with N‐Substituted 3‐Amino‐5,5‐dimethyl‐2‐cyclohexenones.
Authors: Bannikova Yu. N. , Maslivets A. N. , Aliev Z. G. 
Published: May 2005

AbstractFor Abstract see ChemInform Abstract in Full Text.
A Modular, One‐Pot, Four‐Component Synthesis of Polysubstituted 1,3‐Oxazolidines.
Authors: Tejedor David , Santos‐Exposito Alicia , Gonzalez‐Cruz David , Marrero‐Tellado Jose Juan , Garcia‐Tellado Fernando 
Published: May 2005

AbstractFor Abstract see ChemInform Abstract in Full Text.
Functionalization at Position 3 of the Phenyl Ring of the Potent mGluR5 Noncompetitive Antagonists MPEP.
Authors: Alagille David , Baldwin Ronald M. , Roth Bryan L. , Wroblewski Jarda T. , Grajkowska Ewa , Tamagnan Gilles D. 
Published: May 2005

AbstractFor Abstract see ChemInform Abstract in Full Text.
Podospermic Acid, 1,3,5‐Tri‐O‐(7,8‐dihydrocaffeoyl)quinic Acid from Podospermum laciniatum (Asteraceae)
Authors: Zidorn Christian , Petersen Bent O. , Udovicic Vedrana , Larsen Thomas O. , Duus Jens O. , Rollinger Judith M. , Ongania Karl‐Hans , Ellmerer Ernst P. , Stuppner Hermann 
Published: May 2005

AbstractFor Abstract see ChemInform Abstract in Full Text.
Synthesis of Modified Proanthocyanidins: Easy and General Introduction of a Hydroxy Group at C‐6 of Catechin; Efficient Synthesis of Elephantorrhizol.
Authors: Boyer Francois‐Didier , Es‐Safi Nour‐Eddine , Beauhaire Josiane , Le Guerneve Christine , Ducrot Paul‐Henri 
Published: May 2005

AbstractFor Abstract see ChemInform Abstract in Full Text.
Characterization of Amoeba proteus myosin VI immunoanalog
Authors: Dominik Magdalena , Kłopocka Wanda , Pomorski Paweł , Kocik Elżbieta , Rędowicz Maria Jolanta 
Published: May 2005

AbstractAmoeba proteus, the highly motile free‐living unicellular organism, has been widely used as a model to study cell motility. However, molecular mechanisms underlying its unique locomotion and intracellular actin‐based‐only trafficking remain poorly understood. A search for myosin motors responsible for vesicular transport in these giant cells resulted in detection of 130‐kDa protein interacting with several polyclonal antibodies against different tail regions of human and chicken myosin VI. This protein was binding to actin in the ATP‐dependent manner, and immunoprecipitated with anti‐myosin VI antibodies. In order to characterize its possible functions in vivo, its cellular distribution and colocalization with actin filaments and dynamin II during migration and pinocytosis were examined. In migrating amoebae, myosin VI immunoanalog localized to vesicular structures, particularly within the perinuclear and sub‐plasma membrane areas, and colocalized with dynamin II immunoanalog and actin filaments. The colocalization was even more evident in pinocytotic cells as proteins concentrated within pinocytotic pseudopodia. Moreover, dynamin II and myosin VI immunoanalogs cosedimented with actin filaments, and were found on the same isolated vesicles. Blocking endogenous myosin VI immunoanalog with anti‐myosin VI antibodies inhibited the rate of pseudopodia protrusion (about 19% decrease) and uroidal retraction (about 28% decrease) but did not affect cell morphology and the manner of cell migration. Treatment with anti‐human dynamin II antibodies led to changes in directionality of amebae migration and affected the rate of only uroidal translocation (about 30% inhibition). These results indicate that myosin VI immunoanalog is expressed in protist Amoeba proteus and may be involved in vesicle translocation and cell locomotion. Cell Motil. Cytoskeleton 61:172–188, 2005. © 2005 Wiley‐Liss, Inc.
The last but not the least: The origin and significance of trailing adhesions in fibroblastic cells
Authors: Rid Raphaela , Schiefermeier Natalia , Grigoriev Ilya , Small J. Victor , Kaverina Irina 
Published: May 2005

AbstractMature adhesions in a motile fibroblast can be classified as stationary “towing” adhesions in the front and sliding trailing adhesions that resist the traction force. Adhesions formed at the front of motile fibroblasts rarely reach the trailing zone, due to disassembly promoted by intensive microtubule targeting. Here, we show that the majority of adhesions found at the trailing edge originate within small short‐lived protrusions that extend laterally and backwards from the cell edge. These adhesions enlarge by sliding and by fusion with neighboring adhesions. A further subset of trailing adhesions is initiated at a novel site proximal to trailing stress fibre termini. Following tail retraction, trailing adhesions are actively regenerated and the stress fibre system is remodeled accordingly; the tensile forces elaborated by the contractile actin system are consequently redirected according to trailing adhesion location. We conclude that persistent and dynamic anchorage of the cell rear is needed for the maintenance of continuous unidirectional movement of fibroblasts. Cell Motil. Cytoskeleton 61:161–171, 2005. © 2005 Wiley‐Liss, Inc.
Bystander cell proliferation is modulated by the number of adjacent cells that were exposed to ionizing radiation
Authors: Gerashchenko Bogdan I. , Howell Roger W. 
Published: May 2005

AbstractBackgroundDirect cell‐to‐cell contact appears to be a prerequisite for the proliferative response of bystander WB‐F344 cells co‐cultured with irradiated cells; however, neither gap junctional intercellular communication nor long‐range factors released into the medium appear to be involved (Cytometry 2003;56A:71–80). The present work investigated whether the proliferative bystander response depends on the number of irradiated cells (cells exposed to external γ‐rays or cells exposed to short‐range β‐particles emitted by DNA‐incorporated 3H‐thymidine) that are adjacent to unirradiated bystander cells.MethodsSubconfluent monolayers of rat liver epithelial cells (WB‐F344) were incubated in the presence of (methyl‐3H)thymidine at a concentration of 5.8 kBq/ml for 18 h. Radiolabeled cells containing 0.7 × 10−3 Bq/cell (absorbed dose: 0.14 Gy) were plated together with unlabeled cells in proportions of 6% and 94%, 12% and 88%, 25% and 75%, 50% and 50%, and 75% and 25%, respectively, keeping constant the total number of plated cells. In a parallel experiment, cells acutely exposed to 5 Gy of 137Cs γ‐rays were plated with unirradiated cells in the same proportions. In both experiments, cells were co‐cultured for 24 h followed by a flow cytometric study of their proliferation. The two cell populations in the co‐cultures were distinguished by staining one population with carboxyfluorescein diacetate, succinimidyl ester, which metabolizes intracellularly.ResultsIncreasing the fraction of irradiated cells relative to unirradiated bystander cells led to an increase in proliferation of bystander cells. Specifically, in co‐cultures in which irradiated cells were initially mixed with unirradiated cells in proportions of 50% and 50% and of 75% and 25%, respectively, bystander cells showed a statistically significant increase of their proliferation compared with the controls.ConclusionsThe proliferative response of WB‐F344 bystander cells is modulated by the number of adjacent cells that are exposed to ionizing radiation from external γ‐rays or intracellularly emitted 3H β‐particles. © 2005 Wiley‐Liss, Inc.
Protein adsorption at glassy carbon electrodes: The effect of covalently bound surface groups
Authors: Downard Alison J. , Roddick Alisa D. 
Published: May 2005

AbstractA diazonium salt coupling procedure was used to covalently bind various p‐substituted phenyls to glassy carbon electrodes. The response of modified electrodes for oxidation of ferrocenemethanol in the absence and presence of bovine serum albumin was monitored to give a measure of protein adsorption. Carboxylate groups close to the surface did not influence protein adsorption (relative to polished glassy carbon electrodes), however, hydrophobic groups increased adsorption. These results are compared to those for similar experiments at electrochemically pretreated glassy carbon electrodes. Hydrophilic groups attached to the surface via sufficiently long linkages reduced protein adsorption and may be useful for analysis of clinical samples.
Interpreting diffusion coefficients of electrochemical probes in oil‐in‐water microemulsions
Authors: Mackay Raymond A. , Myers Stephanie A. , Brajter‐Toth Anna 
Published: May 2005

AbstractThe relationship between apparent diffusion coefficients, D′, of electroactive probe and thc microstructure of an oil‐in‐water anionic microemulsion, sodium dodecyl sulfate (SDS)/dodecane/I‐pentanol/0.1M NaCIaq has been investigated. Three probes, ferrocene (Fc), Fe(CN) and methyl viologen (MV2+) allowed the effect of ditrerent microstructure and interactions on the D′‐values to be investigated. The results indicate that the droplet as well as hicontinuous microemulsion structures can be identified and point to the effects of cross‐ phase exchange, partitioning, and multiple binding on the D′‐values.
Horizontal two‐dimensional (iso‐dalt) electrophoresis: Use of agarose isoelectric focusing and SDS gel electrophoresis in an exponential gradient for characterization of plasma proteins
Authors: Emerson David L. , Chapuis‐Cellier Colette , Arnaud Philippe 
Published: May 2005

AbstractThe two‐dimensional (iso‐dalt) electrophoresis system for protein separation has been modified to include the use of flat‐bed agarose isoelectric focusing in the first dimension, horizontal SDS‐electrophoresis in an exponential acrylamide gradient in the second dimension, molecular weight standards run side by side with the sample in the SDS‐polyacrylamide gel, and radiolabeled proteins as internal standards. Direct determination of the pH gradient after the first dimension and of molecular weights after the second dimension permits more accurate measurement of the protein spots in both the x and y axes, thus improving the confidence limits of the technique. The reproducibility of molecular weight determinations was calculated for eight different proteins in six different gels, with an overall standard deviation of 3.02%. Incorporation of internal standards is useful in identifying and confirming protein patterns. Examples of the application of this technique to the separation of specific plasma proteins are described.
A comparison of commonly used discontinuous and continuous buffer systems for electrophoresis in sodium dodecyl sulfate‐containing polyacrylamide gels
Authors: Lanzillo Joseph J. , Stevens Joanne , Fanburg Barry L. 
Published: May 2005

AbstractA comparison between commonly used multiphasic zone electrophoresis (MZE) and continuous zone electrophoresis (CZE) buffer systems for polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS‐PAGE) was performed. Some proteins behave differently in one or more of the buffer systems, indicating that buffer choice for SDS‐PAGE may be more important than previously recognized. Guidelines are suggested for choosing buffer systems for purposes other than molecular weight analysis.
Continuous flow electrophoresis: The crescent phenomena revisited Part II: Nonisothermal effects
Authors: Ivory Cornelius F. 
Published: May 2005

AbstractAn asymptotic solution to the partial differential equation governing solute behavior in the continuous flow electrophoresis device is combined with solutions for the convective, electrophoretic and electroosmotic velocities in the chamber under nonisothermal operating conditions. The results illustrate the effect of temperature gradients on the net dispersion of solute in continuous flow electrophoresis. Three modes of operation are tested for this chamber: the convective velocity is in the same direction as gravity, the convective velocity is in the direction opposite to gravity and the effect of gravity is negligible.
A simple procedure for high efficiency counting of labeled protein bands in polyacrylamide slab gels
Authors: Chao Lee , Chao Julie 
Published: May 2005

AbstractA simple procedure is described for counting labeled protein bands after polyacrylamide slab gel electsrophoresis. Proteins labeled with radioisotopes are separated on conventional polyacrylamide slab gels. After fiction and staining, the slab gels are dried onto filter papers under vacuum. The labeled protein patterns are recorded by autoradiography or fluorography. The sample tracks are separated from each other by cutting the dried slab gel lengthwise. Each sample track is cut into predetermined sections by making parallel cuts with a film cutter. The sections are deposited into scintillation vials and digested with 50% hydrogen peroxide. The digested samples are counted in an aqueous scintillator. This procedure provides a direct quantitation of 3h and 14C‐labeled protein bands by reproducibility counting. The results also show that both high resolution and excellent reproducibility are obtainable by this relatively fast and inexpensive method.
Rapid and sensitive location of protein zones in gels using o‐phthaldialdehyde
Authors: Taylor Michael D. , Andrews Anthony T. 
Published: May 2005

AbstractA new fluorescent staining technique using o‐phthaldialdehyde(OPA) has been developed for the rapid post‐electrophoretic location for separated zones of proteins and glycoproteins. The method has also been applied to the detection of immunoprecipitates and, in the form of a spray reagent, to the detection of proteins separated on thin‐layer gel filtration plates. Major protein zones can be visualized within 1–2 min with maximum sensitivity being achieved within 15 min. In polyacrylamide and agarose gels, the sensitivity is of the same order as staining with Coomassie Blue G‐250. Reagents are very inexpensive and, because the reaction is performed at neutral or weekly alkaline pH in aqueous buffers, retention of enzymatic or other biological activity should be optimal. The method is thus particularly suitable for use in preparative applications and when it is desirable to combine general protein detection with specific location of zone of enzyme activity.