Abstract:
:Factor VIII procoagulant protein (VIII:C) purified from commercial factor VIII concentrate contained multiple polypeptides ranging in mol wt from 79,000 to 188,000, all of which were removed from solution by a monoclonal anti-VIII:C antibody specific for a thrombin-sensitive epitope. In a time-course digest of the purified VIII:C using a trace amount of purified human alpha-thrombin, changes occurred in all VIII:C polypeptides during the activation and inactivation of VIII:C activity. The generation and destruction of a mol wt 92,000 polypeptide paralleled the increase and decrease in VIII:C activity, suggesting that this polypeptide represents an activated form. These results provide the basis for a working hypothesis for the mechanism of thrombin activation of VIII:C.
journal_name
Bloodjournal_title
Bloodauthors
Fulcher CA,Roberts JR,Zimmerman TSsubject
Has Abstractpub_date
1983-04-01 00:00:00pages
807-11issue
4eissn
0006-4971issn
1528-0020journal_volume
61pub_type
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