Quantities of ubiquinone bound to proteins in beef heart mitochondria.
Ubiquinone-binding proteins were isolated and purified from heavy beef heart mitochondria. 35% of the total ubiquinone in the mitochondria was associated with the purified proteins. About 83% of the associated ubiquinone could be released from the proteins by proteolytic treatment showing that at least 29% (0.87 nmol/mg) of the total ubiquinone (3.0 nmol ubiquinone/mg) in the mitochondria is in the bound form. The purified ubiquinone-binding proteins were resolved into 5 polypeptides with the molecular weights of 17.4, 12.9, 12.6, 9.8 and 8.6 kD on sodium dodecyl sulfate-gel electrophoresis.
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D008929:Mitochondria, Heart / Q000032:analysis*; D008970:Molecular Weight; D013381:Subtilisins / Q000378:metabolism; D010738:Type C Phospholipases / Q000378:metabolism; D014451:Ubiquinone / Q000378:metabolism*
D002352:Carrier Proteins; C027208:ubiquinone-binding proteins; D014451:Ubiquinone; D010738:Type C Phospholipases; D013381:Subtilisins