A latent thiol proteinase from ascitic fluid of patients with neoplasia.
Pepsin treatment of ascitic fluid from patients with neoplasia generated a cysteine (thiol) proteinase activity which resembles cathepsin B (EC 3.4.22.1) in its requirements for thiol activators, susceptibility to inhibitors and specificity for synthetic substrates. As judged by gel filtration, pepsin reduced the molecular size of the latent enzyme from an Mr of 41,000 to 33,000 after activation. Both forms are larger than human liver cathepsin B. In addition to its presence in ascitic fluid, the pepsin-activated species was found in the medium of ascites cells maintained in culture. The latent enzyme may be an enzyme-inhibitor complex or an inactive precursor of a cathepsin B-like proteinase.
D001201:Ascites / Q000201:enzymology* / Q000209:etiology; D002401:Cathepsin B; D002403:Cathepsins / Q000378:metabolism; D002478:Cells, Cultured; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000378:metabolism*; D005260:Female; D006801:Humans; D007700:Kinetics; D010051:Ovarian Neoplasms / Q000201:enzymology*; D013379:Substrate Specificity
D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D002401:Cathepsin B