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溶藻弧菌的F1-ATP酶。主要亚基的纯化及N端序列

The F1-ATPase of Vibrio alginolyticus. Purification and N-terminal sequence of major subunits.

作者信息

Grinkevich V A, Skulachev V P

机构信息

A.N. Belozersky Laboratory for Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.

出版信息

FEBS Lett. 1989 Dec 4;258(2):219-22. doi: 10.1016/0014-5793(89)81657-6.

DOI:10.1016/0014-5793(89)81657-6
PMID:2532151
Abstract

The F1-type ATPase has been isolated from membrane preparations of marine alkalotolerant bacterium, Vibrio alginolyticus. The enzyme was found to consist of two major subunits of 55 and 58 kDa and at least two minor components (38 and 23 kDa). Amino acid sequences of N-terminal regions of the major subunits revealed close homology with those of E. coli H+-ATPase and of Propionigenium modestum Na+-ATPase.

摘要

已从海洋耐碱细菌溶藻弧菌的膜制剂中分离出F1型ATP酶。发现该酶由两个主要亚基(55 kDa和58 kDa)和至少两个次要成分(38 kDa和23 kDa)组成。主要亚基N端区域的氨基酸序列与大肠杆菌H⁺-ATP酶和适度丙酸杆菌Na⁺-ATP酶的氨基酸序列显示出密切的同源性。

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引用本文的文献

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J Bioenerg Biomembr. 1993 Jun;25(3):285-95. doi: 10.1007/BF00762589.
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Characterization of a membrane-associated ATPase from Methanococcus voltae, a methanogenic member of the Archaea.来自古细菌产甲烷菌沃氏甲烷球菌的一种膜相关ATP酶的特性分析。
J Bacteriol. 1993 Sep;175(17):5677-82. doi: 10.1128/jb.175.17.5677-5682.1993.
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J Bacteriol. 1990 Dec;172(12):6809-17. doi: 10.1128/jb.172.12.6809-6817.1990.
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J Bacteriol. 1992 Nov;174(21):6743-51. doi: 10.1128/jb.174.21.6743-6751.1992.