Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria

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F1F0-ATP synthase from bovine heart mitochondria: development of the purification of a monodisperse oligomycin-sensitive ATPase.

A new procedure for the isolation of ATP synthase from bovine mitochondria has been developed, with the primary objective of producing enzyme suitable for crystallization trials. Proteins were extracted from mitochondrial membranes with dodecyl-beta-D-maltoside, and the ATP synthase was purified from the extract in the presence of the same detergent by a combination of ion-exchange and gel-filt...

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ATP synthase from bovine heart mitochondria: reconstitution into unilamellar phospholipid vesicles of the pure enzyme in a functional state.

A highly purified and monodisperse preparation of proton-translocating F1F0-ATPase from bovine heart mitochondria is an assembly of 16 unlike polypeptides. This preparation has been reconstituted in the presence of various detergents into unilamellar phospholipid vesicles. Incorporation of the enzyme into vesicles increases the ATP hydrolase activity of the enzyme by 10-20-fold, depending on th...

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ATP synthase complex from bovine heart mitochondria. Subunit arrangement as revealed by nearest neighbor analysis and susceptibility to trypsin.

The nearest neighbor relationships of bovine mitochondrial H(+)-ATPase subunits were investigated by the chemical cross-linking approach using the homobifunctional cleavable reagents dithiobis(succinimidyl propionate) and disuccinimidyl tartrate. Cross-linked proteins were resolved by one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Individual subunits were de...

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ATP synthase complex from bovine heart mitochondria. Passive H+ conduction through F0 does not require oligomycin sensitivity-conferring protein.

Oligomycin sensitivity-conferring protein (OSCP) is a water-soluble subunit of bovine heart mitochondrial H(+)-ATPase (F1-F0). In order to investigate the requirement of OSCP for passive proton conductance through mitochondrial F0, OSCP-depleted membrane preparations were obtained by extracting purified F1-F0 complexes with 4.0 M urea. The residual complexes, referred to as UF0, were found to b...

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Preparation and properties of an ATP-Pi exchange complex (complex V) from bovine heart mitochondria.

Using the general procedure for the isolation of complexes I, II, III, and IV from mitochondria or submitochondrial particles, a preparation (complex V) has been isolated from a fifth fraction with very high ATPJ3Pi exchange (350 to 470 nmol . min-’ mg of protein-’ at 30”) and ATPase (8 to 10 pm01 . min.’ . mg of protein-’ at 30”) activities. Preparations of complex V contain 13 major and minor...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 2007

ISSN: 0014-5793

DOI: 10.1016/j.febslet.2007.05.079