作者: Heinrich AQUILA , Wolfgang EIERMANN , Wilfried BABEL , Martin KLINGENBERG
DOI: 10.1111/J.1432-1033.1978.TB12270.X
关键词: Thermolysin 、 Denaturation (biochemistry) 、 Translocator protein 、 Biochemistry 、 Molecular mass 、 Isoelectric point 、 Mitochondrion 、 Trypsin 、 Biology 、 ATP–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).