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首页> 外文期刊>Journal of bacteriology >Purification and properties of two membrane alkaline phosphatases from Bacillus subtilis 168.
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Purification and properties of two membrane alkaline phosphatases from Bacillus subtilis 168.

机译:枯草芽孢杆菌168中两种膜碱性磷酸酶的纯化和性质。

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摘要

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.
机译:从枯草芽孢杆菌168固定相细胞膜中提取了两种碱性磷酸酶,并通过羟磷灰石柱色谱纯化为均质蛋白。碱性磷酸酶I和II在几个特性方面有所不同,例如亚基分子量,底物特异性,热稳定性,Km,pH稳定性和肽图。

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