Characterization of halophilic alkaline phosphatase from Halomonas sp 593, a moderately halophilic bacterium

被引：12

作者：

Ishibashi, M ^{[1
]}

Yamashita, S ^{[1
]}

Tokunaga, M ^{[1
]}

机构：

[1] Kagoshima Univ, Fac Agr, Kagoshima 8900065, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2005年 / 69卷 / 06期

关键词：

Halomonas sp; alkaline phosphatase; halophilic enzyme; moderate halophile;

D O I：

10.1271/bbb.69.1213

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A halophilic alkaline phosphatase was highly purified (about 510-fold with about 21% yield) from a moderate halophile, Halomonas sp. 593. The N-terminal 35 amino acid sequence of this enzyme was found to be more acidic than those previously isolated from Vibrio spp., and this enzyme was partially resistant to SDS. Several enzymatic properties demonstrated that it showed higher halophilicity than those enzymes from Vibrio spp.

引用

页码：1213 / 1216

页数：4

共 21 条

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