Isolation of Thrombin-Like Activity from the Venom of Trimeresurus Okinavensis
- 1 January 1972
- journal article
- Published by S. Karger AG in Pathophysiology of Haemostasis and Thrombosis
- Vol. 1 (1) , 31-43
- https://doi.org/10.1159/000213736
Abstract
An activity that converts bovine fibrinogen to fibrin has been isolated from the crude venom of Trimeresurus Okinavensis by means of gel chromatography and ion exchange chromatography on arginine-Sepharose 6B. A high degree of homogeneity is suggested by gel chromatography, gel electrophoresis, isoelectric focusing and end-group analysis. The purified fraction is an acidic glycoprotein with a molecular weight of about 35,000. It catalyzes the hydrolysis of certain arginine esters, but has very low proteolytic activity towards casein. The fraction has a strong catalytic activity for converting fibrinogen into a fibrin-like compound. A certain factor-X-activating ability persists. It does not activate human factor-XIII zymogen in plasma.Keywords
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