Studies on pancreatic enzymes in fish. X. Enzymic characterization of two carboxypeptidases B from the catfish pancreas.

DOI Web Site 3 Citations
  • YOSHINAKA Reiji
    Department of Fisheries, Faculty of Agriculture, Kyoto University
  • SATO Mamoru
    Department of Fisheries, Faculty of Agriculture, Kyoto University
  • MORISHITA Joji
    Department of Fisheries, Faculty of Agriculture, Kyoto University
  • IKEDA Shizunori
    Department of Fisheries, Faculty of Agriculture, Kyoto University

Bibliographic Information

Other Title
  • ナマズの膵臓カルボキシペプチダーゼBの酵素の性質
  • ナマズの膵臓カルボキシペプチダーゼBの酵素的性質〔英文〕
  • ナマズ ノ スイゾウ カルボキシ ペプチダーゼ B ノ コウソテキ セイシツ

Search this article

Abstract

Two carboxypeptidases B from the pzncreas of the catfish Parasilurus asotus were found to have pH optima of 7.5 and were found to be stable between pH 6.5 and 9.0. Both enzymes were strongly inhibited by EDTA, o-phenanthroline, and cysteine. The enzymes inactivated by EDTA were regenerated almost completely by the addition of ZnCl2. These results indicate that both enzymes are metalloenzymes which require zinc for activity. Both enzymes were found to be able to hydrolyze Bz-Gly-Arg and Bz-Gly-Lys.<br> These results indicate the close similarity between two catfish carboxypeptidases B and suggest that the catfish enzymes are closely related to carboxypeptidases B from other species.

Journal

  • NIPPON SUISAN GAKKAISHI

    NIPPON SUISAN GAKKAISHI 50 (10), 1723-1727, 1984

    The Japanese Society of Fisheries Science

Citations (3)*help

See more

Keywords

Details 詳細情報について

Report a problem

Back to top