Isolation of the cytochrome-bc1 complex from rat-liver mitochondria.
The cytochrome bc1 complex has been isolated from rat-liver mitochondria by two different procedures. The enzyme isolated by either procedure exhibits a specific cytochrome b and cytochrome c1 heme content of approximately 8 and 4 nmol/mg protein respectively. Both preparations contain only seven polypeptides on sodium dodecylsulfate gel electrophoresis, with the following apparent molecular weights: I, 50000; II, 46000; III, 33000; IV, 25000; V, 12500; VI, 10000; VII, 5600. The polypeptide composition is identical to that of the beef-heart enzyme isolated by cholate/ammonium sulfate fractionation. Furthermore, with the exception of subunit II (core protein 2), the apparent molecular weights of the subunits are identical in the rat-liver and beef-heart enzymes.
D000818:Animals; D000968:Antimycin A / Q000494:pharmacology; D003574:Cytochrome c Group / Q000031:analogs & derivatives*; D003575:Cytochromes c1 / Q000302:isolation & purification* / Q000378:metabolism; D004227:Dithionite / Q000494:pharmacology; D004229:Dithiothreitol / Q000494:pharmacology; D046911:Macromolecular Substances; D008297:Male; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight; D010084:Oxidation-Reduction; D051381:Rats; D013053:Spectrophotometry
D003574:Cytochrome c Group; D046911:Macromolecular Substances; D004227:Dithionite; D000968:Antimycin A; D003575:Cytochromes c1; D004229:Dithiothreitol