珍珠鸡（Numida meleagris galeata）碱性磷酸酶的纯化及部分性质

Purification and some of the properties of alkaline phosphatase in guinea fowls (Numida meleagris galeata).

Ukoha A I, Okoh P N, Icce D, Dim N I, Olomu J M

Department of Animal Science, Ahmadu Bello University, Zaria, Nigeria.

Br Poult Sci. 1988 Mar;29(1):27-33. doi: 10.1080/00071668808417023.

Abstract

Alkaline phosphatase activity in the plasma of different strains of guinea fowls showed considerable variation both within and between sexes as well as within and between strains. 2. The enzymes from different strains of wild guinea fowls had different mobilities on disc polyacrylamide electrophoresis but each was characterised by a single band. 3. When the enzyme was purified 163-fold from the plasma of a domesticated grey breasted strain, both ion-exchange chromatography and gel-filtration purification steps yielded a single band of enzyme. 4. The purified enzyme had a molecular weight of 79,400 +/- 3,000 and was stable up to 60 degrees C at the optimum pH of 9.6. 5. Evidence is provided that guinea fowl alkaline phosphatase is a metalloenzyme.

摘要

不同品系珍珠鸡血浆中的碱性磷酸酶活性在性别内和性别间以及品系内和品系间均表现出相当大的差异。2. 不同品系野生珍珠鸡的酶在圆盘聚丙烯酰胺电泳上具有不同的迁移率，但每种酶均以单一条带为特征。3. 当从一只驯化的灰胸品系珍珠鸡的血浆中纯化该酶163倍时，离子交换色谱和凝胶过滤纯化步骤均产生了单一条带的酶。4. 纯化后的酶分子量为79,400±3,000，在最佳pH值9.6时，在60℃下仍稳定。5. 有证据表明珍珠鸡碱性磷酸酶是一种金属酶。