Purification and Properties of Acid Phosphatase in Goat Milk

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  • KUZUYA Yasuo
    Department of Poultry and Animal Sciences, Faculty of Agriculture Gifu University
  • TANAHASHI Tamotsu
    Department of Poultry and Animal Sciences, Faculty of Agriculture Gifu University

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  • 山羊乳の酸性ホスファターゼの精製と性質
  • 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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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.

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