Aug 1, 1989

Epitope of OSCP oligomycin sensitivity conferring protein exposed at the surface of the mitochondrial ATPase-ATPsynthase complex

C GodinotB Roux


Immunological studies were designed to study the structure of the oligomycin sensitivity conferring protein (OSCP) integrated in the mitochondrial ATPase-ATPsynthase complex. The monoclonal antibody 2B1B1 used in this study could bind as well to purified or membrane bound OSCP as shown previously by Protein A-gold immunocytochemistry and by competitive immunotitration. In this paper, it is shown that 2B1B1 can also immunoprecipitate the F0F1 complex from a Triton X-100 extract. This means that not only, 2B1B1 binds to the surface of OSCP but also that the binding of 2B1B1 did not destroy the interactions between F0 and F1 and further demonstrates the external location of the 2B1B1 binding site in the ATPase-ATPsynthase complex. This antigenic site was located on the N-terminal sequence of OSCP, between residues 1 and 72, as demonstrated after chemical cleavage of OSCP with formic acid, hydroxylamine and partial cleavage with cyanogen bromide. The proximity of Tyr and Arg to the epitope was suggested by the lack of 2B1B1 binding to iodinated OSCP and by the susceptibility of this binding to trypsin or to endoproteinase Arg-C treatments of OSCP, respectively. A more precise location of the epitope has been attempted by using the ...Continue Reading

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Mentioned in this Paper

Monoclonal Antibodies
Precipitin Tests
Formicum acidum, formic acid, Homeopathic preparation
Endopeptidase Arg-C
Adenosine Triphosphatases
Antigenic Specificity
Mitochondria, Heart
Cytokinesis of the Fertilized Ovum

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