Thrombin proteolysis of purified factor viii procoagulant protein: correlation of activation with generation of a specific polypeptide.

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

Blood

journal_title

Blood

authors

Fulcher CA,Roberts JR,Zimmerman TS

subject

Has Abstract

pub_date

1983-04-01 00:00:00

pages

807-11

issue

4

eissn

0006-4971

issn

1528-0020

journal_volume

61

pub_type

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