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pubmed-article:2903696pubmed:abstractTextBovine 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.lld:pubmed
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pubmed-article:2903696pubmed:articleTitlePurification and characterization of low-molecular-weight beef heart proteolipids: use of fast atom bombardment-mass spectrometry for identification.lld:pubmed
pubmed-article:2903696pubmed:affiliationLaboratoire de Chimie Organique des Substances Naturelles, UA CNRS 31, Strasbourg, France.lld:pubmed
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