Isolation of an abnormal protein C molecule from the plasma of a patient with thrombotic diathesis.
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.
Faioni
E M
EM
Thrombosis/Hematology Research Program, Oklahoma Medical Research Foundation, Oklahoma City 73104.
Esmon
C T
CT
Esmon
N L
NL
Mannucci
P M
PM
D000328:Adult; D001777:Blood Coagulation / Q000187:drug effects; D002846:Chromatography, Affinity; D004198:Disease Susceptibility; D005260:Female; D006023:Glycoproteins / Q000097:blood; D006801:Humans; D006868:Hydrolysis; D008297:Male; D011486:Protein C / Q000302:isolation & purification / Q000502:physiology; D020151:Protein C Deficiency; D017293:Protein S; D012697:Serine Endopeptidases / Q000097:blood; D013379:Substrate Specificity; D013927:Thrombosis / Q000097:blood* / Q000201:enzymology / Q000235:genetics
D006023:Glycoproteins; D011486:Protein C; D017293:Protein S; D012697:Serine Endopeptidases