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.
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Published version (
Free)
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: ASEAN Journal on Science and Technology for Development
Paper Title
Journal
Date
