A cysteine proteinase secreted from human breast tumours is immunologically related to cathepsin B.
The stable cathepsin B-like cysteine (thiol) proteinase secreted from human breast tumours in culture was shown to be destabilized by mercurial compounds. After such treatment the enzyme cross-reacts in a radioimmunoassay with a monospecific antiserum to human liver cathepsin B. It is suggested that the secreted enzyme may be a precursor form of lysosomal cathepsin B.
D000230:Adenocarcinoma / Q000201:enzymology*; D001943:Breast Neoplasms / Q000201:enzymology*; D002401:Cathepsin B; D002403:Cathepsins / Q000276:immunology*; D003429:Cross Reactions; D003470:Culture Media; D046508:Culture Techniques; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000276:immunology*; D005260:Female; D006801:Humans; D009941:Organomercury Compounds / Q000494:pharmacology; D011863:Radioimmunoassay
D003470:Culture Media; D009941:Organomercury Compounds; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D002401:Cathepsin B