艾美球囊霉的碱性磷酸酶：部分纯化与特性分析
Alkaline phosphatase of Blastocladiella emersonii: partial purification and characterization.
作者信息
Selitrennikoff C P, Sonneborn D R
出版信息
J Bacteriol. 1977 Apr;130(1):249-56. doi: 10.1128/jb.130.1.249-256.1977.
Abstract
Alkaline phosphomonoesterase (EC 3.1.3.1) activity from Blastocladiella emersonii, while displaying typically broad substrate specificity for phosphorylated organic compounds, exhibited nearly complete substrate preference for N-acetylglucosamine-6-phosphate over N-acetylglucosamine-1-phosphate. Enzyme in zoospore extracts was purified 43-fold by differential centrifugation followed by gel filtration (Sephadex G-200) and then by ion-exchange chromatography (diethylaminoethyl-cellulose). The partially purified enzyme displayed an apparent molecular weight (Sephadex G-200) of approximately 170,000. The activity of partially purified enzyme exhibited a pH optimum of pH 8.5, did not require a metal divalent cation, but was inhibitable by ethylenediaminetetraacetic acid. During the life cycle of the organism, the specific activity of the phosphatase decreased slightly during germination and early exponential growth but then increased about 4.5-fold during sporulation. B. emersonii alkaline phosphatase does not appear to be a repressible enzyme.
摘要
艾美球囊霉的碱性磷酸单酯酶（EC 3.1.3.1）活性，虽然对磷酸化有机化合物表现出典型的广泛底物特异性，但对6-磷酸-N-乙酰葡糖胺的底物偏好几乎完全高于1-磷酸-N-乙酰葡糖胺。游动孢子提取物中的酶通过差速离心，然后通过凝胶过滤（葡聚糖G-200），再通过离子交换色谱（二乙氨基乙基纤维素）纯化了43倍。部分纯化的酶显示出约170,000的表观分子量（葡聚糖G-200）。部分纯化酶的活性在pH 8.5时表现出最佳pH值，不需要二价金属阳离子，但可被乙二胺四乙酸抑制。在生物体的生命周期中，磷酸酶的比活性在萌发和早期指数生长期间略有下降，但在孢子形成期间增加了约4.5倍。艾美球囊霉碱性磷酸酶似乎不是一种可阻遏的酶。
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