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Amino acid sequence of the oligomycin sensitivity‐conferring protein (OSCP) of beef‐heart mitochondria and its homology with the δ‐subunit of the F 1 ‐ATPase of Escherichia coli
Author(s) -
Ovchinnikov Y.A.,
Modyanov N.N.,
Grinkevich V.A.,
Aldanova N.A.,
Trubetskaya O.E.,
Nazimov I.V.,
Hundal T.,
Ernster L.
Publication year - 1984
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(84)80036-8
Subject(s) - amino acid , protein subunit , oligomycin , biochemistry , escherichia coli , peptide sequence , homology (biology) , biology , mitochondrion , atpase , chemistry , enzyme , gene
The complete amino acid sequence of the oligomycin sensitivity‐conferring protein (OSCP) of beef‐heart mitochondria is reported. The protein contains 190 amino acids and has a molecular mass of 20 967. Its structure is characterized by a concentration of charged amino acids in the two terminal segments (N 1–77 and C 128–190) of the protein, whereas its central region is more hydrophobic. The earlier reported homology of the protein with the δ‐subunit of E. coli F 1 , based on the terminal amino acid sequences of OSCP, is further substantiated.