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Amino‐terminal amino acid sequence of beef heart mitochondrial coupling factor B
Author(s) -
Kantham Lakshmi,
Raychowdhury Raktima,
Ogata Kathleen K.,
Javed Ali,
Rice John,
Rao Sanadi D.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80819-5
Subject(s) - amino acid , peptide sequence , biochemistry , biology , protein primary structure , operon , chemistry , microbiology and biotechnology , escherichia coli , gene
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 aminoterminus 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.