Abstract
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 delta-subunit of E. coli F1, based on the terminal amino acid sequences of OSCP, is further substantiated.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases*
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Amino Acid Sequence
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Animals
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Biological Evolution
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Carrier Proteins*
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Cattle
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Escherichia coli / enzymology*
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Macromolecular Substances
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Membrane Proteins*
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Mitochondria, Heart / enzymology*
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Mitochondrial Proton-Translocating ATPases
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Oligomycins / pharmacology
Substances
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Carrier Proteins
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Macromolecular Substances
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Membrane Proteins
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Oligomycins
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Adenosine Triphosphatases
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Mitochondrial Proton-Translocating ATPases
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oligomycin sensitivity-conferring protein