大豆プロテイナーゼインヒビターに関する研究
書誌事項
- タイトル別名
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- 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.
収録刊行物
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- 日本食品工業学会誌
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日本食品工業学会誌 19 (11), 514-521, 1972
社団法人 日本食品科学工学会
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詳細情報 詳細情報について
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- CRID
- 1390001206405437184
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- NII論文ID
- 130003966573
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- ISSN
- 00290394
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- データソース種別
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- JaLC
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- 抄録ライセンスフラグ
- 使用不可