Thrombin Proteolysis of Purified Factor VIII Procoagulant Protein: Correlation of Activation With Generation of a Specific Polypeptide

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-cours...

Full description

Saved in:
Bibliographic Details
Published in:Blood 1983-04, Vol.61 (4), p.807-811
Main Authors: Fulcher, Carol A., Roberts, James R., Zimmerman, Theodore S.
Format: Article
Language:English
Subjects:
Antibodies, Monoclonal - immunology
Biological and medical sciences
Blood coagulation. Blood cells
Coagulation factors
Electrophoresis, Polyacrylamide Gel
Enzyme Activation
Factor VIII - isolation & purification
Factor VIII - metabolism
Fundamental and applied biological sciences. Psychology
Humans
Molecular and cellular biology
Peptide Biosynthesis
Sodium Dodecyl Sulfate
Thrombin - metabolism
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 αr-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.
ISSN:0006-4971
1528-0020
DOI:10.1182/blood.V61.4.807.807