Cathepsins J and K: high molecular weight cysteine proteinases from human tissues |
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Authors: | J C Liao J F Lenney |
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Affiliation: | Pharmacology Department, School of Medicine, University of Hawaii, Honolulu, Hawaii 96822 USA |
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Abstract: | 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. |
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Keywords: | Z benzyloxycarbonyl AMC aminomethylcoumarin Bz benzoyl NA naphthylamide CPI plasma cysteine proteinase inhibitor SBTI soybean trypsin inhibitor |
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