Thrombin-catalyzed activation of human coagulation factor V.
K Suzuki, B Dahlbäck, J Stenflo - Journal of Biological Chemistry, 1982 - ASBMB
Human coagulation factor V was purified from freshly frozen plasma by a method that gave
high yields of single chain factor V. The purified protein has an Mr= 330,000 and consists of
a single polypeptide chain with the following NH2-terminal sequence: Ala-Gln-Leu-Gly-Gln-
Phe-Tyr-Val. Limited proteolysis of factor V by thrombin led to formation of factor Va which
has a cofactor activity 25-to 30-fold that of factor V. Two intermediates and four end products
were formed in the course of activation. From the NH2 terminus of factor V the end products …
high yields of single chain factor V. The purified protein has an Mr= 330,000 and consists of
a single polypeptide chain with the following NH2-terminal sequence: Ala-Gln-Leu-Gly-Gln-
Phe-Tyr-Val. Limited proteolysis of factor V by thrombin led to formation of factor Va which
has a cofactor activity 25-to 30-fold that of factor V. Two intermediates and four end products
were formed in the course of activation. From the NH2 terminus of factor V the end products …