Immunochemical demonstration of the iron-sulfur protein in Complex III of mitochondrial electron-transfer chain.
An iron-sulfur protein of Complex III was purified by phenyl-Sepharose column chromatography and DEAE-Sepharose column chromatography. The purified preparation was homogeneous as demonstrated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, and a specific antibody directed against this protein was raised in a rabbit. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by electrophoretic blotting and immunoperoxidase reaction indicated that Complex III possesses a single polypeptide which reacts with the antibody. It was also found that the iron-sulfur center-containing subunits identified so far in Complex I did not cross-react with the antibody, indicating that they are antigenically unrelated to the iron-sulfur protein of Complex III.
D000818:Animals; D002417:Cattle; D004579:Electron Transport; D014450:Electron Transport Complex III; D004591:Electrophoresis, Polyacrylamide Gel; D005779:Immunodiffusion; D007506:Iron-Sulfur Proteins / Q000302:isolation & purification*; D008667:Metalloproteins / Q000302:isolation & purification*; D008929:Mitochondria, Heart / Q000201:enzymology*; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification*; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification*; D011808:Quinone Reductases / Q000302:isolation & purification*
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D009097:Multienzyme Complexes; D009247:NADH, NADPH Oxidoreductases; D011808:Quinone Reductases; D014450:Electron Transport Complex III