The purification and subunit structure of a membrane-bound ATPase from the Archaebacterium Halobacterium saccharovorum.
作者信息
Hochstein L I, Kristjansson H, Altekar W
出版信息
Biochem Biophys Res Commun. 1987 Aug 31;147(1):295-300. doi: 10.1016/s0006-291x(87)80120-1.
PMID:2888461
Abstract
A membrane-bound ATPase from Halobacterium saccharovorum was solubilized using sodium deoxycholate and Zwittergent 3-10 and purified by hydrophobic and ammonium sulfate-mediated chromatography. The enzyme, which had a molecular mass of 350 kDa, was composed of two major (87 and 60 kDa) and two minor (29 kDa and 20 kDa) subunits. The halobacterial ATPases appear to be unlike any other ATPase described to date.
摘要
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