地衣芽孢杆菌碱性磷酸酶。溶解度取决于镁，纯化及特性研究。
Alkaline phosphatase from Bacillus licheniformis. Solubility dependent on magnesium, purification and characterization.
作者信息
Schaffel S D, Hulett F M
出版信息
Biochim Biophys Acta. 1978 Oct 12;526(2):457-67. doi: 10.1016/0005-2744(78)90137-7.
The membrane-associated alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) from Bacillus licheniformis MC14, a facultative thermophile, was purified to homogeneity in buffer containing 0.2 M Mg2+. The alkaline phosphatase purified in this manner is insoluble upon removal of the magnesium by dialysis. This insoluble alkaline phosphatase has been characterized and compared to the previously purified heat-solubilized enzyme (Hulett-Cowling, F.M. and Campbell, L.L. (1971) Biochemistry 10, 1364--1371).
来自兼性嗜热菌地衣芽孢杆菌MC14的膜相关碱性磷酸酶（正磷酸单酯磷酸水解酶（最适碱性），EC 3.1.3.1）在含有0.2 M Mg2+的缓冲液中被纯化至同质。以这种方式纯化的碱性磷酸酶在通过透析去除镁后不溶。已对这种不溶性碱性磷酸酶进行了表征，并与先前纯化的热溶性酶进行了比较（Hulett-Cowling, F.M.和Campbell, L.L.（1971年）《生物化学》10, 1364 - 1371）。
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