假单胞菌属中的伯醇硫酸酯酶
Primary alcohol sulfatase in a Pseudomonas species.
作者信息
Payne W J, Williams J P, Mayberry W R
出版信息
Appl Microbiol. 1965 Sep;13(5):698-701. doi: 10.1128/am.13.5.698-701.1965.
Abstract
An ammonium sulfate-precipitated fraction from cell-free extracts of Pseudomonas C12B grown on a medium containing sodium dodecyl sulfate (SDS) contained alkyl sulfatase increased fourfold in specific activity over the crude. Optimal pH (7.5) and temperature (70 C) for sulfate release were determined with SDS labeled with radioactive sulfur (SDS(35)) as test substrate. Phosphate, arsenate, and certain heavy metal ions inhibited desulfation, whereas Mg(++) and Mn(++) stimulated activity of preparations which had been dialyzed against ethylenediaminetetraacetic acid. Dodecanol was recovered in semiquantitative yield from reaction mixtures containing enzyme and SDS(35). Aryl sulfates, secondary alcohol sulfates, and a phenoxyethyl sulfate failed to serve as substrate for this enzyme.
摘要
在含有十二烷基硫酸钠（SDS）的培养基上生长的铜绿假单胞菌C12B无细胞提取物中，经硫酸铵沉淀得到的一个级分含有烷基硫酸酯酶，其比活性比粗提物提高了四倍。以放射性硫标记的SDS（SDS(35)）作为测试底物，确定了释放硫酸盐的最佳pH（7.5）和温度（70℃）。磷酸盐、砷酸盐和某些重金属离子抑制脱硫作用，而Mg(++)和Mn(++)则刺激了用乙二胺四乙酸透析过的制剂的活性。从含有酶和SDS(35)的反应混合物中以半定量产率回收了十二烷醇。芳基硫酸盐、仲醇硫酸盐和苯氧乙基硫酸盐不能作为该酶的底物。
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