Proteolysis of bovine and human prothrombin and of bovine factor X by rat mast cell proteinase.
The alpha-chymotrypsin-like proteinase from rat peritoneal mast cells (RMCP I) rapidly destroyed the normal clotting activity of purified, calcium-free, bovine prothrombin, human prothrombin and bovine factor X and simultaneously removed similar N-terminal peptides (Mr approximately 5,000) from both prothrombin and the 'light' chain of factor X. The amino acid composition of the peptides agreed with the known composition of the regions of the respective parent molecules where gamma-carboxyglutamic acid residues are situated. Ca2+ ions protected each of the proteins from proteolysis and loss of procoagulant activity. Prolonged incubation in the standard physiological assay medium used for prothrombin or treatment with Echis carinatus venom indicated that the thrombogenic portion of prothrombin survived proteolysis by RMCP I. This restricted proteolysis was confirmed by electrophoretic analysis.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001777:Blood Coagulation / Q000187:drug effects; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism* / Q000494:pharmacology; D005170:Factor X / Q000032:analysis / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D066298:In Vitro Techniques; D008407:Mast Cells / Q000201:enzymology*; D011516:Prothrombin / Q000032:analysis / Q000378:metabolism*; D051381:Rats
D000596:Amino Acids; D011516:Prothrombin; D005170:Factor X; D010450:Endopeptidases