Production of Factor X and Factor Xa variants with thrombin, acutin and by autolysis
Journal
Thrombosis Research
Journal Volume
22
Journal Issue
1-2
Pages
213-220
Date Issued
1981
Author(s)
CHE-MING TENG
Abstract
Research in several laboratories established that β-Factor X, as compared with α-Factor X, has 17 less amino acids and less carbohydrate at the C-terminal end of the heavy chain. Using the purified thrombin-like enzyme acutin, isolated from the snake venom of Agkistrodon acutus, β-Factor X was digested to obtain γ-Factor X and δ-Factor X by shortening the heavy chain from the N-terminal end. β, γ, and δ-Factor X were purified and each one was converted to the same active β-Factor Xa by the purified activator of Russell's viper venom (RVV-X). β-Factor Xa converted to β-Factor Xa-E by autolysis and had esterase activity, but did not function in prothrombin activation. δ-Factor X converted to ε-Factor X by autolysis or with α-chymotrypsin. In the conversion the light chain was reduced in length. The active form obtained with RVV-X was β-Factor Xa-E. By SDS polyacrylamide gel electrophoresis δ-Factor X could not be distinguished from β-Factor Xa. © 1981.
Type
journal article