Zusammenfassung
Homogenat von Rattenhaut wurde durch Gel-Chromatographie an Sephadex G-100 fraktioniert. Dabei wurden viele Enzyme, die Naphthylamide von Aminosäuren hydrolysieren, zum Teil voneinander getrennt. Eines von den Enzymen hatte die Fähigkeit nur die Naphthylamide von Arginin und Lysin zu hydrolysieren, während zwölf andere Aminosäure-Naphthylamide, u. a. Leucin-Naphthylamid, nicht gespaltet wurden. Die enzymatische Hydrolyse von Arginin-Naphthylamid war optimal bei neutralem pH und wurde durch Cl-Ionen aktiviert. Methanol, HgCl2 und p-Chloromercuribenzoat inhibierten die Aktivität der Peptidase, während EDTA und DFP keine Wirkung aufwiesen. Diese Peptidase ähnelt der sog. Aminopeptidase B, die man in vielen Organen der Säugetiere gefunden hat.
Summary
Rat skin homogenate was fractionated using gel filtration on Sephadex G-100, and several enzymes hydrolysing aminoacid naphthylamides were partially separated. One of the enzymes was found to hydrolyse naphthylamides of arginine and lysine but not of the twelve other aminoacids tested, e.g. leucine naphthylamide. The enzymic hydrolysis of arginine naphthylamide was optimal at neutral pH and was markedly enhanced by chloride ions at a concentration of 0.2 M. Methanol and sulfhydryl reagents were effective inhibitors while EDTA and DFP had no effect. This enzyme is similar to aminopeptidase B, an enzyme described earlier in several other mammalian tissues.
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This investigation was supported by a research grant from the Sigrid Juselius Foundation and from the Finnish Medical Council. It forms a part of the research project of the Skin Biology Research Unit in Turku (SBRU).
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Hopsu-Havu, V.K., Jansén, C.T. Peptidases in the skin. Arch. klin. exp. Derm. 233, 1–10 (1968). https://doi.org/10.1007/BF00495689
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DOI: https://doi.org/10.1007/BF00495689