Proteolysis of bovine and human prothrombin and of bovine factor x by rat mast cell proteinase

The α-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 (M approximately 5000) from both proth...

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Veröffentlicht in:	Thrombosis research 1986-11, Vol.44 (3), p.327-337
Hauptverfasser:	Wylie, Alistair R.G., Lonsdale-Eccles, John D., Blumsom, Nigel L., Elmore, Donald T.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - analysis Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Blood Coagulation - drug effects Cattle Chemical Phenomena Chemistry Chromatography, DEAE-Cellulose Electrophoresis, Polyacrylamide Gel Endopeptidases - metabolism Endopeptidases - pharmacology Enzymes and enzyme inhibitors factor X Factor X - analysis Factor X - metabolism Fundamental and applied biological sciences. Psychology Humans Hydrolases Hydrolysis In Vitro Techniques mast cell proteinase Mast Cells - enzymology proteolysis Prothrombin Prothrombin - analysis Prothrombin - metabolism Rats
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