Novel isolation of ubiquinone-binding proteins located in different sites of beef heart mitochondrial respiratory chain.
Ubiquinone-binding proteins were isolated from beef heart submitochondrial particles by a simple fractionation procedure using ethanol and ammonium acetate after solubilization of the particles with deoxycholate. The ubiquinone-binding proteins were further purified by passing them through a column of phenyl-Sepharose CL-4B to eliminate the free form of ubiquinone and hydrophobic proteins such as cytochromes. At least 25% of the total ubiquinone present in the submitochondrial particles was associated with the purified proteins. Applying the same method, ubiquinone-binding proteins could be isolated from complexes I and III.
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002417:Cattle; D004579:Electron Transport; D004591:Electrophoresis, Polyacrylamide Gel; D008929:Mitochondria, Heart / Q000032:analysis / Q000378:metabolism*; D014451:Ubiquinone / Q000378:metabolism*
D002352:Carrier Proteins; C027208:ubiquinone-binding proteins; D014451:Ubiquinone