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Cytochemical demonstrations of protease in human peripheral blood cells by use of new α-naphthyl ester substrates

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Summary

The proteases of human leukocytes were cytochemically studied by use of new α-naphthyl esters, tosyl-l-lysine-α-naphthyl ester (TLNE) and acetyl-l-tyrosine-α-naphthyl ester (ATNE). The hydrolytic activities were strong only in neutrophils, with both substrates. They were inhibited completely by DFP and chymostatin, but not by leupeptin and iodoacetate. These results indicate that chymotrypsin-like enzyme(s), capable of hydrolyzing both substrates, exist in neutrophils.

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Authors and Affiliations

  1. Division of Regulation of Macromolecular Function, Institute for Protein Research, Osaka University Suita, 565, Osaka, Japan

    T. Honda, Y. Hitomi, M. Niinobe & S. Fujii

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  1. T. Honda
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  2. Y. Hitomi
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  3. M. Niinobe
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  4. S. Fujii
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Honda, T., Hitomi, Y., Niinobe, M. et al. Cytochemical demonstrations of protease in human peripheral blood cells by use of new α-naphthyl ester substrates. Histochemistry 77, 299–302 (1983). https://doi.org/10.1007/BF00490892

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  • DOI: https://doi.org/10.1007/BF00490892

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