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Species variations amongst lysosomal cysteine proteinases
Author(s) -
Kirschke Heidrun,
Ločnikar Pavel,
Turk Vito
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81089-3
Subject(s) - cathepsin o , cathepsin a , cathepsin , diazomethane , biochemistry , chemistry , cathepsin h , cathepsin b , enzyme , cathepsin l , substrate (aquarium) , spleen , cathepsin d , microbiology and biotechnology , cathepsin s , cysteine , biology , immunology , ecology , organic chemistry
Properties of cathepsin L from rat liver lysosomes were compared with those of a similar enzyme, cathepsin S from beef spleen. Major characteristics of cathepsin L are the high activity against Z‐Phe‐Arg‐methylcoumarylamide and sensitivity to the fast reacting irreversible inhibitor Z‐Phe‐Phe‐diazomethane. In contrast, cathepsin S hydrolyzes Z‐Phe‐Arg‐methylcoumarylamide only slowly and Z‐Phe‐Phe‐diazomethane cannot be regarded as a potent inhibitor of this enzyme. The differences in the substrate specificity of cathepsin L from rat liver and cathepsin S from beef spleen are discussed in comparison with the substrate specificity of cathepsin B from rat and human liver and beef spleen.