Abstract
Hydrolysis of OSCP of bovine heart mitochondria by proteinase from Staphylococcus aureus V8 was followed by isolation of all individual peptides by means of gel-filtration and HPLC. Structural analysis of the peptides allowed to arrange BrCN-fragments and to reconstruct the complete amino acid sequence of the protein. Comparative structural analysis revealed existence of a certain homology between OSCP and delta- and b-subunits of the E. coli H+-ATPase, which are necessary for interaction of catalytic and proton-conducting parts of the bacterial enzyme.
MeSH terms
-
Adenosine Triphosphatases / analysis*
-
Amino Acid Sequence
-
Animals
-
Carrier Proteins*
-
Cattle
-
Chromatography, Gel
-
Chromatography, High Pressure Liquid
-
Drug Resistance
-
Endopeptidases / metabolism*
-
Hydrolysis
-
Membrane Proteins / analysis*
-
Mitochondria, Heart / enzymology*
-
Mitochondrial Proton-Translocating ATPases
-
Molecular Sequence Data
-
Oligomycins / pharmacology
-
Proton-Translocating ATPases / analysis*
-
Staphylococcus aureus / enzymology
Substances
-
Carrier Proteins
-
Membrane Proteins
-
Oligomycins
-
Endopeptidases
-
Adenosine Triphosphatases
-
Mitochondrial Proton-Translocating ATPases
-
Proton-Translocating ATPases
-
oligomycin sensitivity-conferring protein