Open AccessProthrombin-Sepharose-Purified Factor V and Its Role in Prothrombin Conversion
Author(s) -
Twee-Hee Ong
Publication year - 2017
Publication title -
asean journal on science and technology for development/asean journal on science and technology for development
Language(s) - English
Resource type - Journals
eISSN - 2224-9028
pISSN - 0217-5460
DOI - 10.29037/ajstd.221
Subject(s) - sepharose , prothrombin complex , chemistry , chromatography , thrombin , affinity chromatography , prothrombin complex concentrate , biochemistry , coagulation , biology , medicine , immunology , enzyme , warfarin , platelet , atrial fibrillation
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.