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T.C ONG
Department of Psychology, Faculty of Medicine National University of Singapore, Republic of Singapore
Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Computer Science & IT Mathematics

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Prothrombin-Sepharose-Purified Factor V and Its Role in Prothrombin Conversion T.C ONG
ASEAN Journal on Science and Technology for Development Vol. 3 No. 1 (1986): Vol. 3 No. 1 (1986)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (644.758 KB) | DOI: 10.29037/ajstd.221

Abstract

Bovine Factor V isolated by the method of Esnouf and Jobin (1967) has been further purified by affiniy chromotgraphy through prothrombin-sepharose. Factor V bound quantitative to the prothrombin-sepharose column. There was a 2-fold increase in the average specific activity (260.000 units/mg protein) of the Factor V recovered. Recovery of total Factor V activity and total protein was about 95% and 90% respectively.
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