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Identification in the rat skin and subcutaneous granuloma of an enzyme liberating N-terminal glycyl-proline from peptides

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Zusammenfassung

Eine Peptidase mit der Fähigkeit Glycyl-Prolin aus Glycyl-Prolin-Naphthylamid, Glycyl-Prolyl-Alanin und Glycyl-Prolyl-Alanyl-Alanin freiszusetzen, wurde aus Rattenhauthomogenat durch DEAE-Cellulose-Chromatographie partiell getrennt. Die enzymatische Hydrolyse war optimal bei pH 7,5 und wurde durch Ionen oder SH-Gruppen nicht aktiviert oder inhibiert. Ein gleiches Enzym wurde in subcutanen Fremdkörpergranulomen gefunden und histochemisch in Fibroblasten lokalisiert.

Summary

A peptidase capable of liberating glycyl-proline dipeptide from glycyl-proline naphthylamide, glycyl-prolyl-alanine and from glycyl-prolyl-alanyl-alanine was partially separated from enzymes hydrolysing leucine naphthylamide by subjecting rat skin homogenate to chromatography on DEAE-cellulose. The enzyme was found to be optimally active at pH 7.5 and not to require any easily dissociable cofactors or to be dependent on sulphydryl groups. A similar enzyme was found in subcutaneous foreign-body granuloma tissue. Azo colour was seen mainly in fibroblasts when using diazo coupling reaction for histochemical localization of the enzyme.

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References

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Authors and Affiliations

  1. Department of Anatomy, University of Turku, Turku 3, Finland

    Väinö K. Hopsu-Havu & Tauno O. Ekfors

Authors
  1. Väinö K. Hopsu-Havu
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  2. Tauno O. Ekfors
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Additional information

This report forms part III in our series on “Peptidases in the skin”. It is a part of the research project of the Skin Biology Research Unit in Turku (SBRU). Financial support was obtained as grants from The Sigrid Juselius Foundation and from the Finnish Medical Council to the senior author (V.K.H.-H.).

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Hopsu-Havu, V.K., Ekfors, T.O. Identification in the rat skin and subcutaneous granuloma of an enzyme liberating N-terminal glycyl-proline from peptides. Arch. klin. exp. Derm. 235, 301–307 (1969). https://doi.org/10.1007/BF00510968

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  • DOI: https://doi.org/10.1007/BF00510968

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