Abstract
Sylvén and Snellman1 have reported that highly purified beef spleen cathepsin B catalyses the hydrolysis of both benzoylarginine β-naphthylamide (pH. 6.0 optimum) and leucine β-naphthylamide (pH 7.3 optimum). The latter effect was termed “leucine naphthylamidase” activity. Action on both substrates was attributed to a single enzyme, namely, cathepsin B. Maximal rates of hydrolysis were obtained only when cysteine and EDTA were included in the reaction mixtures, a finding that is consistent with the needs of cathepsin B (ref. 2).
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References
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MCDONALD, J., ZEITMAN, B. & ELLIS, S. Leucine Naphthylamide: an Appropriate Substrate for the Histochemical Detection of Cathepsins B and B′. Nature 225, 1048–1049 (1970). https://doi.org/10.1038/2251048a0
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DOI: https://doi.org/10.1038/2251048a0
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