牛乳アルカリ性ホスファターゼの部分精製とその性質

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タイトル別名
  • Partial Purification and Some Properties of Bovine Milk Alkaline Phosphatase
  • ギュウニュウ アルカリセイ ホスファターゼ ノ ブブン セイセイ ト ソノ セ

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抄録

Alkaline phosphatase from bovine milk has been prepared from skim milk by means of the following techniques; rennet treatment, ammonium sulfate precipitation, butanol extraction, acetone fractionation, Sephadex G-200 gel filtration and ion-exchange chromatography on DEAE-cellulose columns. The activity of isolated enzyme was about 3350-fold as high as that of enzyme present in milk. Polyacrylamide gel electrophoresis indicated that milk contained a single alkaline phosphatase isozyme. The molecular weight was estimated by Sephadex G-200 gel filtration to be 190, 000±10, 000. Enzyme optimum pH was obtained in the range from 9.6 to 9.8. The enzyme was stable between pH 7.0 and 10, 0 standing at 5°C for 24hr. At 33°C for 24hr, however, the stability of the enzyme reduced in a narrow range of pH value (8.0-9.0). Of the divalent metals tested, Mg2+, Mn2+, Co2+, Cd2+ and Ni2+ stimulated the enzyme activity, while Ca2+, Be2+ and Cu2+ exerted inhibitory effect. The metal chelating agents were found to inhibit the enzyme activity. Kinetic studies with purified enzyme showed that periodate(Ki=2.4×10-4 mM) and orthophosphate (Ki=3.0mM) were competitive inhibitors, whereas leucine (Ki=0.2mM) and phenylalanine (Ki=3.7mM) were non-competitive inhibitors.

収録刊行物

  • 日本畜産学会報

    日本畜産学会報 51 (7), 501-510, 1980

    公益社団法人 日本畜産学会

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