Abstract
An enzyme, thrombokinase, has been partially purified from human plasma. Its defining property is the ability to convert prothrombin to thrombin in the absence of other cofactors. This prothrombin-converting activity is independent of residual thrombin and is inhibited by soybean trypsin inhibitor but not by DFP. Various cofactors (polylysine or calcium alone, or beef serum or phospholipid in the presence of calcium) accelerate the conversion of prothrombin by thrombokinase.
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 callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
