金黄色葡萄球菌H中N-乙酰胞壁酰-L-丙氨酸酰胺酶的性质与纯化
Properties and purification of N-acetylmuramyl-L-alanine amidase from Staphylococcus aureus H.
作者信息
Singer H J, Wise E M, Park J T
出版信息
J Bacteriol. 1972 Nov;112(2):932-9. doi: 10.1128/jb.112.2.932-939.1972.
Abstract
The principal autolytic enzyme activity of the cell sap of Staphylococcus aureus H has been purified 400-fold. It is an N-acetylmuramyl-l-alanine amidase. This enzyme has a molecular weight of 8 to 10 x 10(5), a pH optimum of 7.3, an ionic strength optimum of 0.16 m and a K(m) of 10(-3)m murein repeating units.
摘要
金黄色葡萄球菌H细胞液中的主要自溶酶活性已被纯化了400倍。它是一种N - 乙酰胞壁酰 - L - 丙氨酸酰胺酶。这种酶的分子量为8至10×10⁵，最适pH为7.3，最适离子强度为0.16 m，对胞壁质重复单元的米氏常数（Kₘ）为10⁻³ m。
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