[Primary structure of the OSCP-protein, conferring the oligomycin sensitivity to the H+-ATPase complex. II. Hydrolysis of OSCP with proteinase from Staphylococcus aureus and reconstruction of the polypeptide chain].
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.
D000251:Adenosine Triphosphatases / Q000032:analysis*; D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins; D002417:Cattle; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004351:Drug Resistance; D010450:Endopeptidases / Q000378:metabolism*; D006868:Hydrolysis; D008565:Membrane Proteins / Q000032:analysis*; D008929:Mitochondria, Heart / Q000201:enzymology*; D025261:Mitochondrial Proton-Translocating ATPases; D008969:Molecular Sequence Data; D009840:Oligomycins / Q000494:pharmacology; D006180:Proton-Translocating ATPases / Q000032:analysis*; D013211:Staphylococcus aureus / Q000201:enzymology
D002352:Carrier Proteins; D008565:Membrane Proteins; D009840:Oligomycins; D010450:Endopeptidases; D000251:Adenosine Triphosphatases; D025261:Mitochondrial Proton-Translocating ATPases; D006180:Proton-Translocating ATPases; C020439:oligomycin sensitivity-conferring protein
Pervichnaia struktura OSCP-belka, pridaiushchego mitokhondrial'nomu H+-ATP-aznomu kompleksu chuvstvitel'nost' k oligomitsinu. II. Gidroliz OSCP proteinazoĭ iz Staphylococcus aureus i rekonstruktsiia polipeptidnoĭ tsepi belka.