Thromb Haemost 1972; 27(01): 033-042
DOI: 10.1055/s-0038-1649007
Originalarbeiten — Original Articles — Travaux Originaux
Schattauer GmbH

Studies on Blood Coagulation Factor V

VI. The Inactivation of Factor V and Prothrombinase
H. C Hemker
1   Laboratory for Coagulation Biochemistry and Cardiovascular Biochemical Research, Clinic for Internal Medicine, University Hospital, Leiden, The Netherlands
,
M. J. P Kahn
1   Laboratory for Coagulation Biochemistry and Cardiovascular Biochemical Research, Clinic for Internal Medicine, University Hospital, Leiden, The Netherlands
› Author Affiliations
Further Information

Publication History

Publication Date:
29 June 2018 (online)

Summary

The disappearance of factor V-activity from human plasma on storage can be described as a first order reaction with an activation energy of about 44 kcal/mol.

The disappearance of factor V- activity from bovine plasma in vitro is a second order reaction with an activation energy of about 66 kcal/mol.

The inactivation of human prothrombinase during coagulation is a second order reaction; the activation energy is about 10 kcal/mol. It is concluded that this inactivation involves a reaction of the factor V moiety of prothrombinase with free factor V.

 
  • References

  • 1 Bell W. N, Alton H. G. Brain extract as a substitute for platelet suspensions in the thromboplastin generation test. Nature 174: 880 1954;
  • 2 Biggs R, Macfarlane R. G. Human Blood Coagulation and its Disorder. 3rd. ed. Blackwell Scientific publications; Oxford: 1962
  • 3 Blombäck B, Blombäck M. A method for the assay of factor V. Scand. J. clin. Lab. Invest 15: 639 1963;
  • 4 Esnouf M. P, Jobin F. The isolation of factor V from bovine plasma. Bioch. J 102: 660 1967;
  • 5 Hemker H. C, Veltkamp J. J, Loeliger E. A. Kinetic aspects of the interaction of blood clotting enzymes. III. Demonstration of the existence of an inhibitor of prothrombin conversion in vitamin K deficiency. Thrombos. Diathes. haemorrh. (Stuttg) 19: 346 1968;
  • 6 Joly M. A physicochemical approach to the denaturation of proteins. Academic Press, Inc; New York: 1965
  • 7 Kahn M. J. P, Hemker H. G. Studies on blood coagulation factor V. Preparation and properties of an artificial factor V reagent by adsorption with Bastearate. Coagulation. 03. 55 (1970a).
  • 8 Kahn M. J. P, Hemker H. C. Studies on blood coagulation factor V. A partially purified factor V preparation from human plasma. Coagulation. 03. 63 (1970b).
  • 9 Kahn M. J. P, Hemker H. G. Studies on blood coagulation factor V. The interaction of salts of fatty acids and coagulation factors. Thrombos. Diathes. haemorrh. (Stuttg) 22: 417 1969;
  • 10 Kahn M. J. P, Hemker H. G. Studies on blood coagulation factor V. Changes of molecular weight accompanying activation of factor V and the procoagulant protein of Russell’s viper venom. Thrombos. Diathes. haemorrh. (Stuttg) 27: 25 1972;
  • 11 Quick A. J. Congenital hypoprothrombinaemia and pseudo-hypoprothrombinaemia. Lancet 253 (02) 379 1947;
  • 12 Stefanini M. New one-stage procedure for the quantitative determination of prothrombin and labile factor. Amer. J. clin. Path 20: 233 1950;
  • 13 Weiss H. J. A study of the cation and pH-dependent stability of factors V and VIII in plasma. Thrombos. Diathes haemorrh. (Stuttg) 14: 32 1965;
  • 14 Boyer P. D. (edit.): The enzymes. Academic Press; New York and London: 1970