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Vyssokikh, M.Y. et al.

Proteinaceous complexes from mitochondrial contact sites.

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.[1]

References

Proteinaceous complexes from mitochondrial contact sites. 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. Biochemistry Mosc. (1999) [Pubmed]

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