Isolation and partial charcterization of a cytochrome b complex and cytochrome oxidase from yeast mitochondria.
A cytochrome b complex and cytochrome oxidase have been purified 14- and 20-fold respectively from yeast submitochondrial particles by a simple procedure involving their spontaneous precipitation from a deoxycholate extract. The recovery of both proteins was almost quantitative. The specific heme contents were 11 and 8 nmoles/mg protein for the cytochrome b complex and cytochrome oxidase respectively and both were spectrally pure. Sodium dodecyl sulfate gel electrophoresis resolved the cytochrome b complex into seven distinct subunits with molecular weights 42,000, 33,000, 27,500, 23,000, 15,500, 13,000 and 10,500. Cytochrome oxidase contained five bands with molecular weights 42,000, 26,500, 21,000, 14,000 and 10,500.
D003580:Cytochromes / Q000302:isolation & purification*; D003576:Electron Transport Complex IV / Q000302:isolation & purification*; D006418:Heme / Q000032:analysis; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology*; D008970:Molecular Weight; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013053:Spectrophotometry
D003580:Cytochromes; D046911:Macromolecular Substances; D006418:Heme; D003576:Electron Transport Complex IV