Purification and crystal growth of F1-ATPase from pig heart mitochondria
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چکیده
منابع مشابه
Inhibition sites in F1-ATPase from bovine heart mitochondria.
High-resolution crystallographic studies of a number of inhibited forms of bovine F1-ATPase have identified four independent types of inhibitory site: the catalytic site, the aurovertin B-binding site, the efrapeptin-binding site and the site to which the natural inhibitor protein IF1 binds. Hitherto, the binding sites for other inhibitors, such as polyphenolic phytochemicals, non-peptidyl lipo...
متن کاملLarge-scale chromatographic purification of F1F0-ATPase and complex I from bovine heart mitochondria.
A new chromatographic procedure has been developed for the isolation of F1F0-ATPase and NADH:ubiquinone oxidoreductase (complex I) from a single batch of bovine heart mitochondria. The method employed dodecyl beta-delta-maltoside, a monodisperse, homogeneous detergent in which many respiratory complexes exhibit high activity, for solubilization and subsequent purification by ammonium sulphate f...
متن کاملPurification and characterization of monolysocardiolipin acyltransferase from pig liver mitochondria.
In mammalian tissues cardiolipin is rapidly remodeled by monolysocardiolipin acyltransferase subsequent to its de novo biosynthesis (Ma, B. J., Taylor, W. A, Dolinsky, V. W., and Hatch, G. M. (1999) J. Lipid Res. 40, 1837-1845). We report here the purification and characterization of a monolysocardiolipin acyltransferase activity from pig liver mitochondria. Monolysocardiolipin acyltransferase ...
متن کاملThe calcium-binding ATPase inhibitor protein from bovine heart mitochondria. Purification and properties.
Two ATPase inhibitor proteins were isolated together from bovine heart mitochondria by a new procedure; each was purified further. The one inhibitor is a Ca2+-binding protein. It was found to contain 2 cysteine residues/mol as well as threonine and proline residues, all of which the other inhibitor (first isolated by Pullman and Monroy (Pullman, M.E., and Monroy, G. C. (1963) J. Biol. Chem. 238...
متن کاملThe unbinding of ATP from F1-ATPase.
Using molecular dynamics, we study the unbinding of ATP in F(1)-ATPase from its tight binding state to its weak binding state. The calculations are made feasible through use of interpolated atomic structures from Wang and Oster [Nature 1998, 396: 279-282]. These structures are applied to atoms distant from the catalytic site. The forces from these distant atoms gradually drive a large primary r...
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ژورنال
عنوان ژورنال: IUBMB Life
سال: 1996
ISSN: 1521-6543
DOI: 10.1080/15216549600201043