Bovine heart mitochondrial coupling factor B was isolated and purified to homogeneity in its active form. The amino-terminal amino acid sequence of the alkylated protein was determined. Two chains with exactly the same sequence except for the presence of an additional Phe at the amino-terminus on one of them were obtained. The 55 amino acid sequence appears to be largely hydrophilic with several charged amino acid residues. This sequence showed no homology with the E. coli unc operon, oligomycin sensitivity conferring protein, or coupling factor 6 or any protein in the data base.

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http://dx.doi.org/10.1016/0014-5793(90)80819-5DOI Listing

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