大豆プロテイナーゼインヒビターに関する研究

DOI

書誌事項

タイトル別名
  • Studies on Soybean Proteinase Inhibitors
  • Part I. Purification and some properties of acetone insoluble inhibitor
  • (第1報)アセトン不溶インヒビターの精製と性質

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抄録

Six trypsin inhibitors (F1, F2, F3-I, F3-II, F4 and F5) and three α-chymotrypsin inhibitors (F3-II, F4 and F5) were fractionated from crude soybean acetone insoluble inhibitor by gel filtration with Sephadex G-100 and DEAE-Sephadex A-25 chromatography.<BR>The F4 inhibitor was found to be homogeneous by electrophoretic and ultracentrifugic analyses, and strongly inhibited both trypsin and α-chymotrypsin, and had separate binding sites for trypsin and α-chymotrypsin, and was stable at temperature in an acidic pH. Molecular weight and sedimentation constant of the F4 inhibitor were determined to be 8000 and 1.85, respectively. NH2- and COOH-terminal amino acids of the F4 inhibitor were aspartic acid and glutamic acid-asparagine, respectively. The reaction between trypsin and the F4 inhibitor consisted in formation of a dissociable complex.<BR>The chemical and physicochemical properties of the F4 inhibitor were in good agreement with those of Bowman-Birk inhibitor and 1.95 inhibitor.

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