Anion Carriers of Mitochondrial Membranes by F. Palmieri, G. Genchi, V. Zara, C. Indiveri, F. Bisaccia

By F. Palmieri, G. Genchi, V. Zara, C. Indiveri, F. Bisaccia (auth.), Prof. Dr. Angelo Azzi, Dr. Katarzyna A. Nałęz, Dr. Maciej J. Nałęcz, Dr. Lech Wojtczak (eds.)

In order to supply a sensible supplier of many of the biochemical approaches, the intracellular setting is subdivided into cubicles shaped through organelles. Mitochondria serve to revive energy-rich compounds, whereas power is principally ate up within the cytosolic house. Molecules enthusiastic about those metabolic cycles need to pass the mitochondrial membrane through really expert vendors embedded within the internal mitochondrial membrane. All suitable structural and sensible facets of the Anion providers of Mitochondrial Membranes in addition to isolation systems, reconstitution experiments and biogenesis of the providers, kinetics of shipping in addition to the metabolic rules mechanisms are taken care of during this volume.

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The presence of deoxycholate in the medium made it difficult to measure the activity of pyruvate exchange when the freeze-thaw-sonication reconstitution method was used. Therefore, a method of detergent removal with Amberlite XAD-2 beads was applied. Moreover, the major part of deoxycholate was removed before reconstitution by passing the samples through a small Sephadex G-25 column. Table 2 demonstrates the effect of DOC removal. In comparison with control sample of hydroxylapatite eluate, its filtration through Sephadex G-25 column increased the total activity, whilst in the presence of deoxycholate the activity was decreased.

Elsevier Amsterdam, pp 235-256 Miiller M (1983) Lipid-protein and protein-protein interactions in the inner mitochondrial membrane. PhD thesis ETH nr 7392 Miiller M, Cheneval D, Carafoli E (1984) Doxorubicin inhibits the phosphate-transport protein reconstituted in liposomes. A study on the mechanism of the inhibition. Bur J Biochem 140:447-452 Miiller M, Krebs JJR, Cherry RJ, Kawato S (1984) Rotational diffusion of the ADP/ATP translocator in the inner membrane of mitochondria and in proteoliposomes.

This might reflect the observations that in the latter organ some carriers are missing (citrate carrier) or are only expressed to a minor extent (dicarboxylate carrier). Chromatography of the hydroxylapatite eluates on celite resulted in a remarkable purification of the 2-oxoglutarate carrier, expressed by the 4-6 times higher specific exchange activity. The celite eluates, containing still a mixture of different proteins (Fig. 2), were processed further by chromatography on organo-mercurial agarose (Affigel 501).

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