Studies on Blood Coagulation Factor V

M. J. P Kahn; H. C Hemker

doi:10.1055/s-0038-1649006

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1972; 27(01): 025-032
DOI: 10.1055/s-0038-1649006

Originalarbeiten — Original Articles — Travaux Originaux

Schattauer GmbH

Studies on Blood Coagulation Factor V

V. Changes of Molecular Weight Accompanying Activation of Factor V by Thrombin and the Procoagulant Protein of Russell’s Viper Venom

Authors

M. J. P Kahn

¹Laboratory for Coagulation Biochemistry and Cardiovascular Biochemical Research, Clinic for Internal Medicine, University Hospital, Leiden, The Netherlands
H. C Hemker

¹Laboratory for Coagulation Biochemistry and Cardiovascular Biochemical Research, Clinic for Internal Medicine, University Hospital, Leiden, The Netherlands

Abstract

Summary

It is confirmed that a protein from Russell’s viper venom has a direct activating action on human as well as bovine factor V.

Unactivated human factor V has a molecular weight as estimated by gel filtration of ∼410,000, after activation the molecular weight is ∼110,000, thus suggesting the dissociation of a tetramer.

The approximative molecular weight figures for unactivated and activated bovine factor V are 400,000 and 195,000, resp. This suggests the dissociation into a dimer accompanying the process of activation.

Full Text

References

References
1 Andrews P. The gel-filtration behaviour of proteins related to their molecular weight over a wide range. Biochem. J 96: 595 1965;
2 Aoki N, Harmison G. R, Seegers W. H. Properties of bovine Ac-globulin concentrates and methods of preparation. Canad. J. Biochem. Physiol 41: 2409 1963;
3 Bergmeyer H. U. Methoden der enzymatischen Analyse. Verlag Chemie G.m.b.H., Weinheim/Bergstraße. 1962
4 Bergsagel D. E, Nockolds E. R. The activation of proaccelerin. Brit. J. Haemat 11: 395 1965;
5 Cole E. R, Koppel J. R, Olwin J. H. Phospholipid - protein interactions in the formation of prothrombin activator. Thrombos. Diathes. haemorrh. (Stuttg.) 14: 431 1965;
6 Deutsch E. Blutgerinnungsfaktoren. F. Deuticke Verlag, Wien. 1955
7 Esnouf M. P, Jobin F. Lipids in prothrombin conversion. Thrombos. Diathes. haemorrh. (Stuttg). Suppl. 17 103 1965
8 Esnouf M. P, Jobin F. The isolation of factor V from bovine plasma. Biochem. J 102: 660 1967;
9 Esnouf M. P, Williams W. J. The isolation and purification of a bovine plasma protein which is a substrate for the coagulant factor of Russell’s viper venom. Biochem. J 84: 62 1962;
10 Hemher H. C, Kahn M. J. P. Reaction sequence of blood coagulation. Nature. 215 1201 1967
11 Hemher H. G, Kahn M. J. P. Studies on blood coagulation factor V. VI. The inactivation of factor V and prothrombinase. 1970
12 Hemher H. C, Esnouf M. P, Hemher P. W, Swart A. C. W, Macfarlane R. G. Formation of prothrombin converting activity. Nature 215: 248 1967;
13 Hjort P. F. Intermediate reactions in the coagulation of blood with tissue thromboplastin. Scand. J. clin. Lab. Invest 09 Suppl. 27 183 1957;
14 Hussain A. Z, Newcomb T. F. Effects of thrombin on factor V. Ann. Biochem. exp. Med 23: 569 1963;
15 Jobin F, Esnouf M. P. Studies on the formation of the prothrombin converting complex. Biochem. J 102: 666 1967;
16 Kahn M. J. P, Hemher H. G. Studies on blood coagulation factor V. I. The interaction of salts of fatty acids and coagulation factors. Thrombos. Diathes. haemorrh. (Stuttg.) 22: 417 (1970a).
17 Kahn M. J. P, Hemher H. C. Studies on blood coagulation factor V. IV. A partially purified factor V preparation from human plasma. Coagulation 03: 63 (1970b).
18 Lewis M. L. The mechanism of action of human accelerator globulin and its relation to other clotting factors. Blood 09: 520 1954;
19 Macfarlane B. G. The coagulant action of Russell’s viper venom; the use of antivenom in defining its reactions with a serum factor. Brit. J. Haemat 07: 498 1961;
20 Newcomb T. F, Hoshida M. Factor V and thrombin. Scand. J. clin. Lab. Invest. 17, Suppl 84: 61 1965;
21 Papahadjopoulos D, Hougie C, Yin E. T. Purification and properties of bovine factor X, molecular changes during activation. Biochemistry 03: 1931 1964;
22 Rapajport S. Personal communication. Biochemistry 08: 1397 1969;
23 Strässle R. Chromatographie von Thrombin. B. B. A 73: 462 1963;
24 Ware A. G, Murphy R. G, Seegers W. H. The function of Ac-globulin in blood clotting. Science 106: 618 1947;
25 Whittaher J. R. Determination of molecular weights of protein by gel filtration on Sephadex. Analyt. Chem 35: 1950 1953;
26 Williams W. J, Esnouf M. P. The fractionation of Russell’s viper (vipera russellii) venom with special reference to the coagulant protein. Biochem. J 84: 52 1962;