bluuebunny/crossref_metadata_2025_split huggingface dataset:
An Abnormal Fibrinogen in a Venezuelan Family
Authors: Bosch N. B. , Arocha-Piñango G. 
Published: June 2019

An apparently new fibrinogen abnormality, inherited as an autosomal dominant trait, was found in 4 members of a family affected with moderate bleeding. Prolongation of plasma prothrombin, thrombin and Reptilase times and normal concentration of fibrinogen were observed. Normal values of platelet aggregation, FDP and antithrombin III levels were obtained. The k value of the thromboelastogram was slightly increased. Factor XIII was 50 to 60% (Beringwerke F XIII kit) and 100% by radial inmuno diffusion. Photometric study of thrombin induced polymerization of fibrin in plasma or purified fibrinogen and the aggregation of monomers in plasma measured by a two stage method, were abnormal. Marked prolongation of the clotting time of fibrin monomers were observed at pH over 7.4. Alterations of polymerization curves and plasma thrombin time were accentuated by raising molarity and ameliorated by Ca ions, increasing thrombin concentration and frozen storage. Normal plasma was slightly inhibited by patient’s plasma in these tests.Normal electrophoretic mobility of the abnormal fibrinogen was shown on cellulose acetate, Polyacrylamide and inmunoelectrophoresis. Ouchterlony inmunodiffusion revealed non-identity pattern with normal fibrinogen.
Thrombin and Reptilase Induced Fibrin Structures in the Presence of Dextran: A Quantitative Electron Microscope Study
Authors: Krause W. H. , Zimmermann P. 
Published: June 2019

The present study describes an electron microscopic analysis, using a quantitative morphometric method, of fibrin network obtained by thrombin and reptilase in the presence of dextran. The thickness of the thrombin induced fibrin meshwork show a significant difference compared to fibrin formed by reptilase. The segment length of reptilase fibrin are reduced to 25% and the thickness of the fibers are reduced to 75% in comparison with thrombin fibrin.The thickness of the fibrin meshwork obtained by thrombin and/or reptilase in the presence of dextran (

w 40,000) is significantly diminished compared to saline controls (p < 0.001). Segment length and thickness of fibers in the clots with dextran showed different results when thrombin or reptilase were used as enzyme.The investigation indicates that the fibrin meshwork formed by thrombin and/or reptilase in the presence or absence of dextran result in a significantly different fibrin morphylogy. The results are different to the so far descriptive electron microscopic studies.
Inhibition of Human Platelet Aggregation by the Proteolytic Effect of Streptokinase (SK). Role of the Factor VIII Related Antigen
Authors: Castillo R. , Maragall S. , Guisasola J. A. , Casals F. , Ruiz C. , Ordinas A. 
Published: June 2019

Defective ADP-induced platelet aggregation has been observed in patients treated with streptokinase. This same effect appears “in vitro” when adding SK to platelet rich plasma (PRP). Classic hemophilia and normal platelet poor plasmas (PPP) treated with SK inhibit the aggregation of washed platelets; plasmin-treated normal human serum also shows an inhibitory effect on platelet aggregation. However, von Willebrand SK-treated plasmas do not inhibit the aggregation of washed platelets. The same results appear when plasmas are previously treated with a rabbit antibody to human factor VIII.This confirms that the antiaggregating effect is mainly linked to the digested factor VIII related antigen.The inhibition of ADP-induced platelet aggregation has been proved in gel filtration-isolated and washed platelets from SK-treated PRP.Defective ristocetin-induced platelet aggregation has also been observed- This action does not appear in washed platelets from SK-treated PRP in presence of normal PPP, but it does in presence of SK-treated PPP, which suggests that the inhibition of the ristocetin-induced aggregation is due to the lack of factor VIII and not to the factor VIII-related products.Heparin, either “in vivo” or “in vitro”, has corrected the antiaggregating effect of SK.
Duration of the Inhibition Effect of Acetylsalicylic Acid on Human Platelet Function
Authors: Baele G. , Verdonck L. , Vermeulen A. , Barbier F. 
Published: June 2019

Six useful parameters of the release reaction are measured in 10 human volunteers prior to Aspirin® intake and 1,4,5,6 and 7 days after a single ingestion of 1 gram Aspirin®. These parameters include the intensity of aggregation after 5 min by diluted collagen (ΔE5) and after 10 min by Thrombofax® (ΔE10) and the serotonin-14C release by undiluted and diluted collagen, by Thrombofax® and by bovine plasma.Although a significant inhibition (Wilcoxon signed rank test) is found one day after the Aspirin® ingestion, the duration of the inhibition effect is different according to the test used. The inhibition of the aggregation and serotonin-14C release by Thrombofax® is no longer present on the 4th day. The inhibition effect is found till the 4th day using the serotonin-e14C release by bovine plasma, till the 5th day using the Serotonine-14C release by undiluted collagen and till the 6th day using the aggregation intensity by diluted collagen. The duration of the inhibition is most prolonged (till the 7th day included) if serotonin-14C release by diluted collagen is measured. Individual differences in intensity and duration of the ASA effect on the platelets are noted.In conclusion, the methods for studying the modification of the platelets by acetyl-:salicylic acid are different in sensitivity as to the duration of the inhibition effect after a single oral ingestion. A combination of different tests allows an easier detection of an ASA effect in a single patient.
Comparison of the Effects of Some Anorectic Drugs on Platelet and Brain 5-Hydroxy-Tryptamine (5 HT) in Rats
Authors: Roncaglioni C. , Buczko W. , Samanin R. , Gaetano G. de , Garattini S. 
Published: June 2019

A number of anorectic drugs have been studied for their effects on the uptake and release of 5 HT in platelets and on the levels of brain 5 HT and 5-hydroxyindolacetic acid (5HIAA) in the rat. Platelet studies have been performed in vitro, whereas brain levels have been measured after drug administration. Phentermine (α-dimethylphenylethylamine), die-thylpropion (2-diethylamino propiophenone) and d-amphetamine sulphate showed no effect on the above parameters. Mazindol (5(p-chlorophenyl)-2-5-dihydro-3H-imidazo-(2-1-α)isoindol-5-01) inhibited 5HT uptake by platelets, but neither induced release of 5HT from platelets nor modified 5HT or 5HIAA levels in the brain. Both d-fenfluramine H-Cl and 4-chloroamphetamine-HCl inhibited 5HT uptake by platelets, induced release of platelet-bound 5HT and lowered brain 5HT and 5HIAA levels. S 922 (trifluoro-methylphenyl(benzoyloxy)ethylamino-2-propane), a congener of fenfluramine, was inactive as an inhibitor of 5 HT uptake, was a weak releaser of 5 HT from platelets but effectively reduced 5HT and 5HIAA levels in the brain. This drug is rapidly metabolized in vivo to form fenfluramine.The in vivo effects of anorectic drugs on brain 5 HT levels seem therefore correlated with the capacity of these drugs to release in vitro 5 HT from platelets rather than with their in vitro inhibitory activity on platelet 5HT uptake.Supported by Grants 1ST. 73-00400-04 and H. 73-00218-31 of the Italian Research Council (C.N.R.).
Anticoagulation During Six Hours of Extracorporeal Perfusion. Comparison between Heparinization and Defibrinogenation
Authors: Berglin E. , Hansson H.-A. , Teger-Nilsson A.-C. , William-Olsson G. 
Published: June 2019

Four dogs were given heparin and four other dogs were defibrinogenated with Defibrase®. The dogs were then perfused for six hours with a membrane oxygenator. Capillary bleeding tendency was measured with a standardized skin-flap technique. Platelet accumulation in the lungs and on the oxygenator membranes was examined with 51Cr-labelled platelets and with scanning electron microscopy. Fibrin deposits on the oxygenator membranes were examined with immunoelectrophoresis after plasmic degradation. Pump flow, gas transfer across the oxygenator membrane and coagulation data were followed.Capillary bleeding from the skin-flap was more pronounced in the dogs treated with heparin than in the defibrinogenated dogs. The 51Cr-labelled platelets accumulated in the lungs and on the membranes of both groups, but more pronounced in the heparinized animals. Scanning electron microscopy confirmed the findings for oxygenator membranes. Both groups of animals had fibrin deposits on the membranes with wide individual variations. There was no difference between the two groups concerning gas exchange across the oxygenation membranes. The pump flow was higher in the defibrinogenated dogs (mean flow 38-64 ml/min and kg bw) than in the heparinized ones (mean flow 22-40 ml/min and kg bw).Anticoagulation with Defibrase® might be an alternative to heparin during prolonged extracorporeal perfusion.
Inhibition of Ristocetin-Induced Platelet Aggregation (RIPA) by Haemaccel® and Fibrinogen
Authors: Stibbe J. , Kirby E. 
Published: June 2019

RIPA was investigated using purified human factor VIII (F VIII) and formalin-treated washed platelets suspended in tris buffered saline. At constant (F VIII), aggregation was very sensitive to the conc, of Ristocetin (R) in the range 0.2-0.5 mg/ml, but higher (R) did not further increase aggregation. At constant (R), increasing (F VIII) caused increased aggregation for any (F VIII) used (0.3-3.0 μg protein/ml, 0.015-0.15 U F Vlll-related ant ig en/ml).RIPA was inhibited by low conc. (0.15 mg/ml) of the gelatin plasma expander Haemaccel (H) (Behringwerke). Addition of H after aggregation was complete caused reversal of the aggregation. The inhibition could be overcome by increasing (R), but not by increasing (F VIII) in the conc, ranges used. The conc, of R which overcame H inhibition also caused precipitation of H. This precipitation could be reversed by increasing (H). Our evidence suggests that H inhibits RIPA by binding R, thus inhibiting the interaction of R and F VIII on the platelet surface which is responsible for aggregation.Human Fibrinogen (Fb) (Kabi, 99% pure, 0.5 U F Vlll-related antigen/mg) caused a similar inhibition of RIPA in conc, as low as 0.2 mg/ml. Higher conc caused greater inhibition, which could be overcome by increasing (R). The Fb (2.5 mg/ml) itself did not induce aggregation in the presence of R. R may also bind to other plasma proteins as well since it can form a precipitate with serum.These findings are of considerable importance for the quantitative measurement of the Ristocetin co-factor. RIPA is very sensitive to a small range of (R) and the availability of R in the test system can be greatly affected by the presence of Fb and other plasma proteins.
Effect of Phospholipase C on Human Platelets
Authors: Otnœss A.-B. 
Published: June 2019

The effect on human platelets of phospholipase C (Bacillus cereus) has been studied. Platelets prepared by gel filtration lost 20-30% of their phospholipids when incubated with phospholipase C for 20 min. Phosphatidylethanolamine (PE) was reduced by about 50%, whereas phosphatidylcholine and phosphatidylserine were reduced each by about 20%. Sphingomyelin was not reduced.These data suggest an asymmetrical distribution of phospholipids in the platelet membrane, PE being more accessible and therefore probably mainly located in the outer part of the membrane.The loss of phospholipids was not accompanied by aggregation, nor did the platelets lose their ability to aggregate with thrombin or ADP. Data on release of serotonin, platelet factor 3 and 4 and scanning electron micrographs of treated platelets will be given.
Repeated Phlebographies for Follow-Up of Deep Vein Thrombi
Authors: Gruber U.F. , Hongler Th. , Jung W. , Hutter O. , Steinmann E. , Schmitt H. 
Published: June 2019

In a prospective, randomised, controlled study comparing the effectiveness of minidose heparin and dextran 40 for reducing deep vein thrombosis (DVT) after major surgery, we have shown that in the control group 36% of the 107 patients so far studied develop DVT, 13% of the 105 patients in the heparin group and 20% of the 104 in the dextran group. Both heparin and dextran show a statistically significant effect. In addition we carry out repeated phlebographies in all patients developing DVT as proven by the fibrinogen test. Immediately after the diagnosis is made, a first phlebography is carried out, a second one 14 days later. Results:Only 1 thrombus, in a heparin patient, increased in size.It is hoped to gain further insight into the course of an established thrombus and how it is influenced by drugs as s.c. heparin and dextran by continuing this extremely time-consuming and difficult study, since it is not easy to carry out repeated phlebographies in the same patient.
A Randomized Comparative Study on Early Prophylactic Treatment of Thrombosis Using Heparin and High-Molecular Dextran Following Injuries of the Lower-Leg
Authors: Gaudernak T. , Kuderna H. , Olbert F. , Pelinka H. , Schlag G. 
Published: June 2019

A randomized study was carried out on 50 patient suffering from lesions in the lower segment of the leg (fractures and ruptures of Achilles tendon). The patients were divided into two groups treated with Heparin (3x5000 i.u./die) and Dextran - 70 500 ml/die. respectively.The incidence of thrombosis was as high as 44%. In all cases, however, it remained limited to the veins of the tibial region. No significant difference was found between Heparin and Dextran patients.Control by phlebography carried out after one year in 38 patients indicated rechannelling of the affected veins in all patients. It also showed deep lesions of the veins in the form of a post-thrombotic syndrom (II/2) in three patients.This leads to the conclusion that immediate administration of Heparin or Dextran — 70 is strongly to be recommended for patients suffering from a recent fracture in the tibial region as a prophylactic measure against thrombosis. It greatly reduces the incidence of pulmonary emboli or of the frequent post-thrombotic syndrome.
Activation of Endotoxin-Induced Intravascular Coagulation in Congenitally C6-Deflcient Rabbits
Authors: Lohmann Elke , Müller-Berghaus G. 
Published: June 2019

Activation of endotoxin-induced coagulation is thought to be caused by platelet factor 3. Since the release of platelet factor 3 after mixing platelets and endotoxin is dependent on the presence of complement factors, studies were performed in rabbits congenitally deficient in the sixth component of complement (C6). Endotoxin infusion (40 μg/kg × hr) caused a decrease in platelet counts in C6-deficient as well as in normal rabbits. Furthermore, after endotoxin infusion activation of intravascular coagulation occurred in C6-deficient rabbits to the same degree as in normal rabbits : prothrombin time and partial thromboplastin time were prolonged, factor V- and factor VII-activities were decreased, and ethanol gelation tests revealed positive results. Nine out of 10 C6-deficient rabbits demonstrated fibrin-rich microdots in the glomerular capillaries. Since platelet factor 3 is not released by endotoxin in the C6-deficient rabbits, these experiments make it likely that the release of platelet factor 3 does not represent the trigger mechanism of endotoxin-induced intra-vascular coagulation.(Supported by the Deutsche Forschungsgemeinschaft, Bad Godesberg, Germany.)
Factor VIII, Small Active Factor VIII Fragments, and von Willebrand Factor
Authors: Wagner R. H. 
Published: June 2019

Factor VIII activity of human, canine, and bovine preparations is associated with a molecule of high molecular weight. These preparations dissociate almost completely in 0.25 M Ca2+, yielding a small active fragment with factor VIII activity, and a high molecular weight fraction (carrier protein) with almost no factor VIII activity. With Ca2+ absent, the small active fragment recombines with the carrier protein to form a large protein with factor VIII activity. Mixtures of normal human small active fragment with human hemophilic carrier protein give normal recombination. Comparable experiments with human von Willebrand and canine “carrier protein fractions” show no recombination. The data suggest a working model of a small active fragment(s) linked by noncovalent bonds to a carrier molecule, comprised of repeating subunits, deficient in von Willebrand’s disease.Thrombin increases the activity of factor VIII preparations or the small active fragment obtained by Ca2+ dissociation. When a factor VIII preparation is treated with thrombin and subjected to gel chromatography or ultracentrifugation, the factor VIII activity appears to be associated with a small molecule. Factor VIII activity of this small molecule is not enhanced by thrombin. These and other data will be discussed.
Mechanism of the Prolonged Bleeding Time in yon Willebrand’s Disease (vWd)
Authors: Mannucci P. M. , Holmberg L. , Ruggeri Z. M. , Nilsson I. M. 
Published: June 2019

Factor-VIII antigen was characterized by means of an immunofluorescence technique in biopsy specimens obtained at dental extractions from the buccal mucosa of ten patients with vWd. No activity could be elicited in five patients with severe recessive vWd, whereas venules and arterioles stained positively in five patients with a moderate form characterized by dominant pattern of inheritance. In six patients, immunofluorescence was also carried out in specimens obtained after cryoprecipitate infusion at a time when the plasma defects (VIIIAHF, VIIIAGN and VIIIVWF) were corrected but the long bleeding time was not modified. No activity was detectable on the vessel wall of those patients who were negative before the infusion. It is suggested that the defect of primary hemostasis in patients with vWd is related to the vascular contents of factor-VIII related properties rather than to their plasmatic levels.Supported by grants from the Fondazione Angelo Bianchi Bonomi, the Swedish Research Council and the Faculty of Medicine, University of Lund.
The Histochemical Assay of Plasminogen Activator in the Venous Wall - An Inter-Ethnic Study
Authors: Franz R. B. , Hugo N. , Jansen C. R. 
Published: June 2019

Despite intensive research in the field of blood coagulation and fibrinolysis facilitated by several studies emanating from this continent, the results still afford no satisfactory explanation for the well established observation of the relative rarity of clinically manifest venous thrombo-embolic disease in the Black African.Pandolfi’s modification of the “fibrinolytic autograph” method of Todd was selected to assess the histochemical localization and the degree of activator activity in the venous wall of the upper and lower limbs in a White control group (18) and in a group of 20 Black patients.Both ethnic groups showed greater fibrinolytic activity in the veins of the upper limb - a difference which appeared to satisfy the test of actuarial cross examination (P < 0,00001). Of particular interest was the significantly greater fibrinolytic activity in the lower limb of the African patients as compared with the lower limb veins of the White group (P < 0,05).The increased fibrinolytic activity in the lower limb veins in Black Africans may be an additional anti-thrombogenic component in the haemostatic profile of this particular ethnic group.
Detection of Carriers of Hemophilia by Hemorrhagometry
Authors: Jesdinsky-Buscher J. , Sutor A. H. , Niederhoff H. 
Published: June 2019

Hemorrhagometry, a new in-vivo method, measures bleeding time, intensity and total blood loss from a small standardized wound (Sutor et al.: Blut 22, 27, 1971). In patients with hemophilia these values are within the normal range when the test is performed at room temperature (24° C). However, when the wound is cooled to 17° C (cold tolerance test), bleeding time is abnormally long in hemophiliacs. Therefore, we investigated this test in carriers of hemophilia. The cold tolerance test was performed in 16 ‘proven’ and 6 ‘probable’ carriers (criteria according to Nilsson). 14 proven and 4 probable carriers showed abnormal bleeding times of 15 min and more (2 proven carriers of hemophilia B did not differ markedly from 20 carriers of hemophilia A). When hemorrhagometry was performed at room temperature, the carriers could not be distinguished from normal control persons.Of 15 sisters and aunts of hemophiliacs 9 had abnormal cold tolerance test findings, in fair agreement with the probability of .5 to be expected theoretically. Thus the hemorrhagometry cold tolerance test is helpful in detecting carriers of hemophilia.
High Fibrinogen Concentrations and a Positive Ethanol Gelation Test
Authors: Slaastad R. A. , Godal H. C. 
Published: June 2019

In patients with a positive ethanol gelation test other findings indicating consumption coagulopathy was more frequently demonstrated than in patients with a negative test. Furthermore, high fibrinogen levels were closely associated with a positive test, even, when all the other parameters studied were normal.To see if high concentrations of fibrinogen alone produced gelation with ethanol fibrinogen was administered intravenously to rabbit. During infusion of highly purified fibrinogen, the test remained negative even at fibrinogen levels above 1500mg%. If the fibrinogen was treated with traces of thrombin prior to infusion, the ethanol test became positive at fibrinogen values about 500 mg%. Thus, soluble fibrin is necessary to give a positive ethanol test even at high fibrinogen levels. This was also supported by in vitro studies.
The Value of a Prothrombin Complex Concentrate in the Coagulation Defect of Liver Disease
Authors: Thomson Jean M. , Poller L. , Green G. , Dymock I. W. 
Published: June 2019

A prothrombin complex concentrate rich in factor VII has been used in the management of the clotting defect in thirteen patients with liver disease. Adequate correction of coagulation was achieved immediately after the infusion in all cases. Within four hours there was some deterioration and by twenty-four hours the results approximated to pre-infusion values. Liver biopsy procedures were performed without haemorrhagic complication in the immediate post-infusion period. There was no evidence of induced intravascular coagulation.Other prothrombin complex concentrates have proved disappointing both in their failure to correct the clotting defect and their production of DIC. From our results the use of this factor “VII rich concentrate appears to be the treatment of choice in patients with liver disease requiring temporary correction of the coagulation defect.
Thromboplastin and Platelet Factor 3: Protein and Phospholipid Components Required for Procoagulant Activity
Authors: McCoy L. E. , Liu D. T. H. , Wu V. Y. 
Published: June 2019

Characteristics of bovine brain and lung thromboplastins and platelet factor 3 are compared, emphasizing protein and phospholipid moieties involved in procoagulant activity. Isolated tissue and platelet procoagulant lipoproteins were separated into lipid and protein fractions by repeated ethanolic extraction. Lipid composition and quantitation was ascertained by thin layer chromatography. The protein-free lipid mixture functioned as a partial thromboplastin. Protein fractions were purified by deoxycholate solubilization, gel filtration, and chromatography on diethylaminoethyl cellulose. Comparative biochemical properties were determined by gel filtration, Polyacrylamide gel electrophoresis, sedimentation velocity and by carbohydrate and amino acid composition. Purified protein components were devoid of enzymatic activity. They were also free of procoagulant activity on prothrombin or au top roth rombin III (Factor X) unless they were combined with one or more phosphatides of ethanolamine (PE), choline (PC), serine (PS), or inositol (PI). The proteins of thromboplastin appear to have homologous biochemical characteristics and phospholipid requirements for expression of proeoagulant activity, while differences in platelet factor 3 activity relate to differences in both protein and phospholipid requirements.(Supported by USPHS, NIH Grant HL 14142).