The purification and subunit structure of a membrane-bound ATPase from the Archaebacterium Halobacterium saccharovorum.
L I Hochstein, H Kristjansson, W Altekar
Index: Biochem. Biophys. Res. Commun. 147 , 295-300, (1987)
Full Text: HTML
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.
Related Compounds
Related Articles:
2010-03-15
[Bioorg. Med. Chem. 18 , 2225-31, (2010)]
Characterizing synthetic polymers and additives using new ionization methods for mass spectrometry.
2014-06-15
[Rapid Commun. Mass Spectrom. 28(11) , 1175-84, (2014)]
2014-08-01
[J. Virol. 88(16) , 9361-78, (2014)]
Isolation and preparation of chloroplasts from Arabidopsis thaliana plants.
2008-01-01
[Methods Mol. Biol. 425 , 171, (2008)]
A comparative analysis of polyurethane hydrogel for immobilization of IgG on chips.
2007-06-05
[Anal. Chim. Acta 592 , 132, (2007)]