The contribution of bovine Factor V and Factor Va to the activity of prothrombinase.
TLDR
The present data indicate that the model prothrombinase described in this paper consists of a phospholipid-bound, stoichiometric complex of Factor Va and Factor Xa, with bound Factor Va serving as the "binding site" for Factor V, in concert with its proposed role in platelets.About:
This article is published in Journal of Biological Chemistry.The article was published on 1979-11-10 and is currently open access. It has received 576 citations till now. The article focuses on the topics: Prothrombinase & Factor X.read more
Citations
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Journal ArticleDOI
Mechanisms of Thrombus Formation
Bruce Furie,Barbara C. Furie +1 more
TL;DR: This review is an account of recent advances in the understanding of the mechanisms of thrombus formation, with emphasis on two independent pathways: one involving primarily platelets and the other initiated by tissue factor.
Journal ArticleDOI
Binding of vascular anticoagulant alpha (VAC alpha) to planar phospholipid bilayers.
Harry A. M. Andree,Chris P. M. Reutelingsperger,Rudolf Hauptmann,H.C. Hemker,W. T. Hermens,George M. Willems +5 more
TL;DR: The ability to mediate VAC alpha binding to 20% DOPS/80% DOPC bilayers was highly specific for Ca2+, and Zinc ions had a synergistic effect on Ca2(+)-dependent VACalpha binding.
Journal ArticleDOI
Platelets and Thrombin Generation
TL;DR: Examination of evidence that platelets play a major role in localizing and controlling the burst of thrombin generation leading to fibrin clot formation concludes that changes in lipid composition are necessary but not sufficient to account for platelet surface regulation of thROMbin generation.
Journal ArticleDOI
In vitro and in vivo studies of the novel antithrombotic agent BAY 59-7939—an oral, direct Factor Xa inhibitor
Elisabeth Perzborn,Strassburger J,Wilmen A,Jens Pohlmann,Susanne Roehrig,Schlemmer Kh,Alexander Straub +6 more
TL;DR: BAY 59‐7939 inhibited endogenous FXa more potently in human and rabbit plasma than rat plasma, correlating with the 14‐fold lower IC50 ofFXa inhibition in rabbit compared with rat plasma; this may suggest a correlation between FXa inhibition and antithrombotic activity.
Journal ArticleDOI
The structural biology of expression and function of tissue factor.
TL;DR: Analysis of the structural biology of TF provides insights into the both the expression of the gene and the function of this cell surface receptor in the initiation of the coagulation protease cascades.
References
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Journal ArticleDOI
A simple method for the preparation of homogeneous phospholipid vesicles.
TL;DR: The homogeneity of vesicle dispersions, prepared by this new method, is examined by several physical techniques and found to be comparable to the best samples prepared by molecular-sieve chromatography.
Book ChapterDOI
[2] Titration of trypsin, plasmin, and thrombin with p-nitrophenyl p′-guanidinobenzoate HCl☆
Theodore Chase,Elliott Shaw +1 more
Journal ArticleDOI
The Mode of Action of Vitamin K IDENTIFICATION OF γ-CARBOXYGLUTAMIC ACID AS A COMPONENT OF PROTHROMBIN
TL;DR: It has been unambiguously demonstrated that the glutamic acid of the glutamylserine has been substituted by carboxylation of the γ carbon atom so that the dipeptide structure is modified and Presumably, the incorporation of the second γ-carboxyl group is dependent on vitamin K.
Journal ArticleDOI
Properties of the factor Xa binding site on human platelets.
TL;DR: An antibody that inhibits both human and bovine coagulation Factor V activity blocks both Xa binding to released platelets and the rapid thrombin formation associated with this binding, suggesting that Factor V from platelets is involved in the Xa-platelet interaction.