Species variations amongst lysosomal cysteine proteinases

FEBS Letters

Ločnikar, Pavel²  Turk, Vito²  Kirschke, Heidrun¹ 

[1] Physiologisch-chemisches Institut, Martin-Luther-Universität Halle-Wittenberg, DDR-4020 Halle (Saale, DDR (Tlx No. 4239);Departmentof Biochemistry, J. Stefan Institute, E. Kardelj University, 61000 Ljubljana, Yugoslavia

关键词: Substrate specificity;    Enzyme differentiation;    Cysteine proteinase;    Cathepsin B;    Cathepsin L;    Cathepsin S;    Bz-;    benzoyl;    -CHN2;    diazomethane;    E-64;    L-3-carboxy-trans-2;    3-epoxypropyl-L-leucylamido(4-guanidino)butane;    -NMec;    7-(4-methyl)coumarylamide;    -NNap;    2-naphthylamide;    -NNapOMe;    2-(4-methoxy)naphthylamide;    Z-;    benzyloxycarbonyl;   

DOI  :  10.1016/0014-5793(84)81089-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown