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  • Title: Species variations amongst lysosomal cysteine proteinases.
    Author: Kirschke H, Locnikar P, Turk V.
    Journal: FEBS Lett; 1984 Aug 20; 174(1):123-7. PubMed ID: 6468652.
    Abstract:
    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.
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