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反刍月形单胞菌赖氨酸脱羧酶的纯化及性质

Purification and properties of Selenomonas ruminantium lysine decarboxylase.

作者信息

Kamio Y, Terawaki Y

出版信息

J Bacteriol. 1983 Feb;153(2):658-64. doi: 10.1128/jb.153.2.658-664.1983.

Abstract

Selenomonas ruminantium, a strictly anaerobic, gram-negative bacterium isolated from sheep rumen, contains lysine decarboxylase (Y. Kamio et al., J. Bacteriol. 145:122-128, 1981). This report describes the synthesis, purification, and characterization of the enzyme. Lysine decarboxylase was synthesized in cells grown in chemically defined medium without lysine. The enzyme was purified approximately 1,800-fold to electrophoretic homogeneity. The native enzyme of approximate molecular weight 88,000 consisted of two identical subunits, each with a molecular weight of 44,000. Several properties of the enzyme were determined and compared with those of the lysine decarboxylases from Escherichia coli and Bacterium cadaverisis.

摘要

反刍月形单胞菌是一种从绵羊瘤胃中分离出的严格厌氧的革兰氏阴性菌,它含有赖氨酸脱羧酶(Y. 神尾等人,《细菌学杂志》145:122 - 128,1981年)。本报告描述了该酶的合成、纯化及特性。赖氨酸脱羧酶是在不含赖氨酸的化学限定培养基中生长的细胞内合成的。该酶被纯化了约1800倍达到电泳纯。天然酶的分子量约为88,000,由两个相同的亚基组成,每个亚基的分子量为44,000。测定了该酶的一些特性,并与大肠杆菌和尸毒杆菌的赖氨酸脱羧酶的特性进行了比较。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e7ed/221682/32f2ee746a69/jbacter00249-0091-a.jpg

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