Prothrombin-Sepharose-Purified Factor V and Its Role in Prothrombin Conversion

Authors

Ong T.C

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.

Publication Date

11-17-2017

Recommended Citation

T.C, Ong (2017) "Prothrombin-Sepharose-Purified Factor V and Its Role in Prothrombin Conversion," ASEAN Journal on Science and Technology for Development: Vol. 3: No. 1, Article 3.
DOI: https://doi.org/10.29037/ajstd.221
Available at: https://ajstd.ubd.edu.bn/journal/vol3/iss1/3