Proteinaceous complexes from mitochondrial contact sites |
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Authors: | Vyssokikh M Y Goncharova N Y Zhuravlyova A V Zorova L D Kirichenko V V Krasnikov B F Kuzminova A E Melikov K C Melik-Nubarov N S Samsonov A V Belousov V V Prischepova A E Zorov D B |
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Institution: | Belozersky Institute Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia. zorov@energ.genebee.msu.su. |
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Abstract: | A Triton X-100 extract from rat brain mitochondria was obtained using low detergent/protein ratio. From this extract a proteinaceous complex was purified; its molecular weight was as high as 880 kD. The complex contained both hexokinase and creatine kinase activity. When incorporated into phospholipid bilayer membranes, the complex formed a channel whose activity was different than the channel activity of purified porin isolated either by adsorption chromatography or by dissociation from protein complexes. A ligand of the mitochondrial benzodiazepine receptor (Ro5-4864) in submicromolar concentrations had an apparent influence on the kinetic behavior of enzymatic coupling of hexokinase and creatine kinase. It is suggested that the 880-kD complex is formed by mitochondrial contact sites. The role of the isolated protein complex in the formation of nonspecific permeability in mitochondria is discussed. |
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