枯草芽孢杆菌168中两种膜碱性磷酸酶的纯化及性质
Purification and properties of two membrane alkaline phosphatases from Bacillus subtilis 168.
作者信息
Sugahara T, Konno Y, Ohta H, Ito K, Kaneko J, Kamio Y, Izaki K
机构信息
Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.
出版信息
J Bacteriol. 1991 Mar;173(5):1824-6. doi: 10.1128/jb.173.5.1824-1826.1991.
Abstract
Two alkaline phosphatases were extracted from the membranes of Bacillus subtilis 168 stationary-phase cells and purified as homogeneous proteins by hydroxyapatite column chromatography. Alkaline phosphatases I and II differed in several properties such as subunit molecular weight, substrate specificity, thermostability, Km, pH stability, and peptide maps.
摘要
从枯草芽孢杆菌168静止期细胞的膜中提取了两种碱性磷酸酶，并通过羟基磷灰石柱色谱法将其纯化为均一蛋白质。碱性磷酸酶I和II在亚基分子量、底物特异性、热稳定性、米氏常数、pH稳定性和肽图等几个特性方面存在差异。
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