MONOMERIC ALKALINE-PHOSPHATASE OF VIBRIO-CHOLERAE
MONOMERIC ALKALINE-PHOSPHATASE OF VIBRIO-CHOLERAE
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DOI：
10.1128/jb.150.3.1033-1039.1982
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发表时间：
1982-01-01
影响因子：
3.2
通讯作者：
DAS, J
中科院分区：
文献类型：
--
作者：
ROY, NK;GHOSH, RK;DAS, J
从2株霍乱弧菌中纯化了碱性磷酸酶。来自两种菌株的酶是MW 60，000的单一多肽。这两种酶的最适pH值约为8.0，可以作用于各种有机磷酸酯，葡萄糖-1-磷酸是最好的底物。这些酶不能水解ATP和AMP。尽管它们具有相同的Km值，但以磷酸对硝基苯酯为底物时，这两种酶的Vmax显着不同。这两种酶对EDTA、Pi和金属离子的敏感性以及脱辅基酶的活性也不同。Ca ~（2+）对脱辅基酶的激活作用最强。
Alkaline phosphatase was purified to homogeneity from 2 strains of V. cholerae. The enzymes from both strains are single polypeptides of MW 60,000. Both enzymes have pH optima around 8.0 and can act on a variety of organic phosphate esters, glucose-1-phosphate being the best substrate. The enzymes are unable to hydrolyze ATP and AMP. Although they have identical Km values, the 2 enzymes differ significantly in Vmax with p-nitrophenyl phosphate as substrate. The 2 enzymes also differ in their sensitivity to EDTA, Pi and metal ions and activities of the apoenzymes. Ca2+ reactivated the apoenzymes most effectively.