Purification and characterization of low-molecular-weight beef heart proteolipids: use of fast atom bombardment-mass spectrometry for identification.
Bovine cardiac muscle was extracted by an acidic chloroform/methanol mixture. A combination of gel permeation and ion-exchange chromatographies in organic solvents and HPLC allowed the purification of subunits VIIIa (Mr 5400) and VIIIb (Mr 4900) of cytochrome c oxidase and of A6L protein (Mr 7900) of ATP synthase. The identification of the proteins was made possible by measurement of their molecular weight by fast atom bombardment-mass spectrometry (FAB-MS) in conjunction with conventional Edman degradation. The determination by FAB-MS of the molecular weight of A6L protein confirmed its supposed formylated N-terminal methionine.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003576:Electron Transport Complex IV / Q000302:isolation & purification; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009206:Myocardium / Q000032:analysis*; D011487:Protein Conformation; D011510:Proteolipids / Q000302:isolation & purification*; D006180:Proton-Translocating ATPases / Q000302:isolation & purification
D011510:Proteolipids; D003576:Electron Transport Complex IV; D006180:Proton-Translocating ATPases