The degradation of bovine and human prothrombin by human polymorphonuclear leukocyte cathepsin G.
Cathepsin G, isolated from human polymorphonuclear leukocytes, was found to effect rapid and specific degradation and biological inactivation of bovine and human prothrombin in the absence of calcium ions with the formation of two peptide fragments from the N-terminal end of the molecule. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate indicated that the molecular weights of the fragments were 5,000 and 17,500. Proteolysis of prothrombin by cathepsin G was inhibited by calcium ions. Leukocyte proteinases such as cathepsin G may be responsible for haemorrhagic disorders associated with myelocytic leukaemia and septicaemia.
D000596:Amino Acids / Q000032:analysis; D000626:Aminopeptidases / Q000378:metabolism; D000818:Animals; D001777:Blood Coagulation / Q000187:drug effects; D018826:CD13 Antigens; D056649:Cathepsin G; D002403:Cathepsins / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002848:Chromatography, DEAE-Cellulose; D006801:Humans; D009504:Neutrophils / Q000032:analysis; D011516:Prothrombin / Q000032:analysis / Q000378:metabolism*; D012697:Serine Endopeptidases
D000596:Amino Acids; D011516:Prothrombin; D002403:Cathepsins; D000626:Aminopeptidases; D018826:CD13 Antigens; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G