Interaction of anti-iron-sulfur protein and anti-ubiquinone binding protein antibodies with complex III of beef heart mitochondria.
Ubiquinol-cytochrome c reductase activity of Complex III was substantially inhibited by anti-iron-sulfur protein antibody, whereas it was not affected by anti-ubiquinone binding protein antibody. Enzyme-linked immunosorbent assay indicated that anti-ubiquinone binding protein antibody do not bind to the complex, but that it binds to Complex III of which iron-sulfur protein and phospholipids have been depleted. These results indicate that some of the antigenic sites of the iron-sulfur protein are located on the surface of Complex III, while the antigenic sites of the ubiquinone binding protein are inaccessible to antibody owing to the interaction with iron-sulfur protein and/or phospholipids in the complex.
D000818:Animals; D002352:Carrier Proteins / Q000276:immunology*; D002417:Cattle; D014450:Electron Transport Complex III; D004797:Enzyme-Linked Immunosorbent Assay; D007506:Iron-Sulfur Proteins / Q000276:immunology*; D046911:Macromolecular Substances; D008667:Metalloproteins / Q000276:immunology*; D008929:Mitochondria, Heart / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000276:immunology*; D011808:Quinone Reductases / Q000276:immunology*
D002352:Carrier Proteins; D007506:Iron-Sulfur Proteins; D046911:Macromolecular Substances; D008667:Metalloproteins; D009097:Multienzyme Complexes; C027208:ubiquinone-binding proteins; D011808:Quinone Reductases; D014450:Electron Transport Complex III