Cathepsins J and K: high molecular weight cysteine proteinases from human tissues.
Human tissue extracts contained two high Mr proteinases active in hydrolyzing the fluorogenic substrate Cbz-phe-arg-aminomethylcoumarin. By gel filtration chromatography, cathepsins J and K had apparent molecular weights of 230,000 and 650,000, respectively. Both enzymes were cysteine proteinases with optimum activity at pH 6.2-6.8; neither had aminopeptidase activity. Human kidney, lung and spleen were rich sources of these enzymes, while liver contained moderate amounts. Cathepsins J and K were partially characterized and appeared to differ from the mammalian high Mr cysteine proteinases described in the literature. In rat liver and kidney and in mouse liver, cathepsin J was localized in the particulate fraction, whereas cathepsin K was not detected in these tissues.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D002122:Calcium Chloride / Q000494:pharmacology; D002164:Camphor / Q000378:metabolism; D056657:Cathepsin K; D002403:Cathepsins / Q000032:analysis*; D002733:Chlorophenols / Q000378:metabolism; D002850:Chromatography, Gel; D003546:Cysteine Endopeptidases; D004229:Dithiothreitol / Q000494:pharmacology; D004338:Drug Combinations / Q000378:metabolism; D004492:Edetic Acid / Q000494:pharmacology; D010450:Endopeptidases / Q000032:analysis*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008099:Liver / Q000201:enzymology; D008970:Molecular Weight; D051381:Rats
D002733:Chlorophenols; D004338:Drug Combinations; D002164:Camphor; C029804:camphorated parachlorophenol; D000255:Adenosine Triphosphate; D004492:Edetic Acid; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; C043569:cathepsin J; C534130:CTSK protein, human; D056657:Cathepsin K; C534132:Ctsk protein, mouse; C534133:Ctsk protein, rat; D002122:Calcium Chloride; D004229:Dithiothreitol