The purification and subunit structure of a membrane-bound ATPase from the Archaebacterium Halobacterium saccharovorum.
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.
D000251:Adenosine Triphosphatases / Q000302:isolation & purification*; D006217:Halobacterium / Q000201:enzymology*; D046911:Macromolecular Substances; D008970:Molecular Weight; D006180:Proton-Translocating ATPases / Q000302:isolation & purification*
D046911:Macromolecular Substances; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases