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A sulphydryl-dependent and chloride-activated peptidase (cathepsin C) that hydrolyses alanyl-alanine naphthylamide

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A peptidase, capable of hydrolysing naphthylamides of alanyl-alanine, leucyl-leucine and glycyl-phenylalanine, as well as amides of glycyl-phenylalanine and glycyl-tyrosine, with a dipeptide and naphthylamine or ammonia as reaction products, was partially purified from hog kidney tissue. The enzyme preparation did not hydrolyse amino acid naphthylamides. The purification procedure included acid precipitation of particles, ammonium sulphate fractionation, gel filtration on Sephadex G 200 and chromatography on DEAE-cellulose. The enzyme was shown to be optimally active at pH 5.0–6.0, dependent on sulphydryl groups, and activated by chloride ions. It was heat stable at 60°C, its isoelectric point was between 4.8 and 6.0, and its molecular weight was 134,000 as determined on gel filtration. The enzyme was suggested as being identical to cathepsin C (E.C. 34. 4. 9).

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Authors and Affiliations

  1. Department of Anatomy, University of Turku, Finland

    V. K. Hopsu-Havu & P. Rintola

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  1. V. K. Hopsu-Havu
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  2. P. Rintola
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Hopsu-Havu, V.K., Rintola, P. A sulphydryl-dependent and chloride-activated peptidase (cathepsin C) that hydrolyses alanyl-alanine naphthylamide. Histochem J 1, 1–17 (1968). https://doi.org/10.1007/BF01054289

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  • DOI: https://doi.org/10.1007/BF01054289

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