Purification and characterization of four trypsin inhibitors from seeds of okra, Abelmoschus esculentus L.

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  • OGATA Fusahiro
    Department of Chemistry, Faculty of Science, Kyushu University
  • IMAMURA Hiroshi
    Department of Chemistry, Faculty of Science, Kyushu University Present address: New Drug Research & Development Department, Pharmaceutical Division
  • HIRAYAMA Kouichirou
    Department of Chemistry, Faculty of Science, Kyushu University
  • MAKISUMI Satoru
    Department of Chemistry, Faculty of Science, Kyushu University

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説明

Four trypsin inhibitors were isolated from seeds of okra (Abelmoschus esculentus L.) and named okra trypsin inhibitors (OTI) A, B, C, and D. The molecular weights of all the inhibitors were estimated to be about 20, 000 by gel filtration on Sephadex G-100 and SDS-polyacrylamide gel electrophoresis. All of these inhibitors inhibited bovine trypsin strongly with the formation of complexes at a 1:1 molar ratio and three (OTI-A, OTI-B, and OTI-C) of them also weakly inhibited bovine chymotrypsin, but not simultaneously. Subtilisin Carlsberg, pronase, papain, and porcine pepsin were not inhibited by these inhibitors. The trypsin inhibitory activity of all four inhibitors was suppressed by treatment with 1, 2-cyclohexanedione but not with 2, 4, 6-trinitrobenzenesulfonate, suggesting that each of the inhibitors contains an arginine residue at the reactive site.

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