Isolation of the ADP/ATP Translocator from Beef Heart Mitochondria as the Bongkrekate‐Protein Complex

作者: Heinrich AQUILA , Wolfgang EIERMANN , Wilfried BABEL , Martin KLINGENBERG

DOI: 10.1111/J.1432-1033.1978.TB12270.X

关键词: ThermolysinDenaturation (biochemistry)Translocator proteinBiochemistryMolecular massIsoelectric pointMitochondrionTrypsinBiologyATP–ADP translocase

摘要: 1 The isolation of the ADP/ATP translocator from beef heart mitochondria as bongkrekate-protein complex is described, using hydroxyapatite chromatography and gel filtration in Triton X-100 solution. 2 The inhibitor bound to protein prior solubilization with detergent for protection against denaturation. Only intact passes easily through column. Bongkrekate shields contrast carboxyatractylate only partially proteinases present crude extract. 3 The isolated bongkrekate shows same molecular weights dodecylsulfate X-100, amino acid composition isoelectric point earlier carboxyatractylate-protein complex. It differs by its higher sensitivity trypsin thermolysin. 4 The identity both proteins demonstrated interconversion into carboxyatractylate-protein. The process requires catalysis ADP or ATP, natural substrates protein. 5 The formation extractable [3H]bongkrekate-protein presence ATP. 6 These data, immunological studies presented earlier, differences reactivity –SH groups complexes (to be published) indicate that represent different conformational states (m-state c-state).

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