Purification and properties of blood-coagulating protease from Cephalosporium sp.
Open Access
- 1 January 1977
- journal article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 41 (2) , 293-298
- https://doi.org/10.1271/bbb1961.41.293
Abstract
Blood-coagulating protease produced extracellularly by Cephalosporium sp. was purified. The purified enzyme moved homogeneously with a sedimentation constant, S20, W of 2.90 s by ultracentrifugation and gave a single protein band on the polyacrylamide gel electrophoresis. The enzyme was an EDTA-sensitive alkaline protease and Ca2+ stabilized its activity. Molecular weight of the enzyme was estimated as 39, 000 by Svedberg's method and 124, 000 by Andrews' method. The enzyme was considered to activate Factor X to Xa. The specific blood-coagulating activity of the enzyme was 1/5 of that of bovine thrombin.Keywords
This publication has 0 references indexed in Scilit: