山羊乳の酸性ホスファターゼの精製と性質

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書誌事項

タイトル別名
  • Purification and Properties of Acid Phosphatase in Goat Milk
  • ヤギニュウ ノ サンセイ ホスファターゼ ノ セイセイ ト セイシツ エイブン

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抄録

Acid phosphatase has been purified from goat milk. After Amberlite CG-50 treatment, the active fractions were purified by gel filtration with a column of Sephadex G-100. The purified enzyme was almost 11700 times as much as the activity present in goat milk. On polyacrylamide gel electrophoresis, the final preparation showed one broad protein band. Enzyme optimum pH was obtained in the range from 4.78 to 4.86. Km for p-nitrophenyl phosphate was 0.83mM at pH 4.70, 0.86mM at pH 4. 85 and 1.12mM at pH 5.10. At pH 4.85 orthophosphate (Ki=2.1mM) and pyrophosphate (Ki=1.15 mM) were competitive inhibitors, whereas KF (Ki=0.23mM) was non-competitive inhibitor.

収録刊行物

  • 日本畜産学会報

    日本畜産学会報 48 (7), 354-360, 1977

    公益社団法人 日本畜産学会

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