Isolation of an abnormal protein C molecule from the plasma of a patient
with thrombotic diathesis
EM Faioni, CT Esmon, NL Esmon and PM Mannucci
Thrombosis/Hematology Research Program, Oklahoma Medical Research
Foundation, Oklahoma City 73104.
Protein C has been purified from the plasma of a patient with thrombotic
diathesis. Both before and after isolation, the protein showed reduced
capacity to hydrolyze synthetic substrates and to anticoagulate plasma.
Proteolysis with the soluble thrombin- thrombomodulin complex proceeded
normally and to completion as judged by sodium dodecyl
sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting.
Approximately one-third of the protein is functional, indicating a
heterozygous defect. Indirect studies suggest that the abnormal component
can bind to protein S and phospholipids. Both forms of activated protein C
can also incorporate radiolabeled diisopropylfluorophosphate.
Volume 71,
Issue 4,
pp. 940-946,
04/01/1988
Copyright © 1988 by The American Society of Hematology
