PMID: 6108210Sep 1, 1980Paper

Reconstitution of mitochondrial oligomycin and dicyclohexylcarbodiimide-sensitive ATPase

European Journal of Biochemistry
E GlaserL Ernster

Abstract

1. Oligomycin and dicyclohexylcarbodiimide-sensitive ATPase was isolated from beef-heart mitochondria and treated with 3.5 M NaBr in order to remove F1. The residue, called F0, was found to consist of seven components. Five of these are stained by Coomassie blue after dodecylsulfate-polyacrylamide-gel electrophoresis. Two of them correspond to the oligomycin-sensitivity-conferring protein and coupling factor F6, with apparent molecular weights of 21,000 and 9,400, respectively. Three additional polypeptides of molecular weights 23,000, 10,500 and 8,600 were not identified with known proteins. Two components not stained with Coomassie blue were detected by autoradiography of the gels of F0 preincubated with [14C]dicyclohexylcarbodiimide. These two components probably represent monomeric and oligomeric forms of the dicyclohexylcarbodiimide-binding protein. 2. F0 induced an oligomycin and dicyclohexylcarbodiimide-sensitive enhancement of K+ + valinomycin-driven proton translocation across the membrane of artificial phospholipid vesicles. 3. The interaction of F0 with purified, soluble beef heart F1 was investigated. F0 was capable of binding F1 and conferring oligomycin and dicyclohexylcarbodiimide sensitivity and cold stability o...Continue Reading

References

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Citations

Dec 1, 1981·Journal of Bioenergetics and Biomembranes·F Guerrieri, S Papa
Feb 1, 1982·Journal of Bioenergetics and Biomembranes·J HoustĕkZ Drahota
Jan 1, 1983·The Journal of Membrane Biology·A E Senior, J G Wise
Mar 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·D R SanadiA Srivastava
Aug 16, 1990·Biochemical and Biophysical Research Communications·B Hamasur, E Glaser
Mar 8, 2008·The EMBO Journal·Mike StraussWerner Kühlbrandt
Sep 15, 1982·Biochimica Et Biophysica Acta·L N Wu, R R Fisher
Dec 15, 1986·Biochemical and Biophysical Research Communications·B NorlingL Ernster

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