大豆プロテイナーゼインヒビターに関する研究

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タイトル別名
  • Studies on Soybean Proteinase Inhibitors
  • Part II. Reduction with borohydride of disulfide bonds and heat denaturation of acetone insoluble inhibitor
  • (第2報)アセトン不溶インヒビターのS-S結合の水素化ホウ素ナトリウムによる還元および熱変性について

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The chemical reactivity of the disulfide bonds toward 0.1 M sodium borohydride and heat denaturation of the F4 inhibitor (Bowman-Birk inhibitor) were studied.<BR>The disulfide bonds were completely reduced at 25°C for 1-2 hours, and the remaining inhibitory activities toward trypsin and α-chymotrypsin were 0-5% and 10-20%, respectively. At 0°C, most of the disulfide bonds were reduced for 5-7 hours, and the remaining inhibitory activities toward trypsin and α-chymotrypsin were 15% and 20%, respectively.<BR>One disulfide bond could be reduced at 0°C for 75 minutes without loss of inhibitory activity toward both trypsin and α-chymotrypsin.<BR>The solutions of the F4 inhibitor in 0.001 M HCl were heated at 100-200°C for 20 minutes. Depression of the inhibitory activity occurred at 135-140°C. At 200°C, the remaining inhibitory activity toward trypsin was 30-40%, whereas α-chymotrypsin inhibitory activity hardly remained.<BR>The disulfide bonds were more or less affected by heat with the rise of temperature, and 1.3 M sulfhydryl groups were formed at 200°C for 20 minutes.

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