Abstract
The atractyloside binding capacity of rat heart mitochondria, but not the binding affinity, was markedly decreased by preincubation of the mitochondria with valinomycin in isotonic KCl medium. Maximum inhibition was attained with 5 ng of valinomycin per mg of mitochondrial protein; it corresponded to a 40% decrease of the atractyloside binding capacity. The inhibitory effect of valinomycin was maximal between pH 7.0 and 7.5. It was more marked for heart mitochondria than for liver mitochondria. Valinomycin inhibition of atractyloside binding to heart mitochondria was counteracted by nigericin and FCCP, by sublytic concentrations of cationic surfactants such as cetyltrimethylammonium bromide, and by low concentrations of trivalent and divalent metal ions at acidic pH's still compatible with atractyloside binding, i.e., down to pH 5.5; trivalent metal ions were more effective than divalent metal ions. The effect of valinomycin was also counteracted by exceedingly high concentrations of K+ (more than 300 mM), resulting in a substantial increase in the ionic strength. These results were discussed in terms of the relation between the atractyloside binding capacity of the inner mitochondrial membrane and the surface potential of this membrane.
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References
Adam, H. (1963a). InMethods in Enzymatic Analysis (Bergmeyer, H. V., ed.), Academic Press, New York, pp. 539–543.
Adam, H. (1963b). InMethods in Enzymatic Analysis (Bergmeyer, H. V., ed.), Academic Press, New York, pp. 573–577.
Aiuchi, T., Kamo, N., Kurihara, K., and Kobatake, Y. (1977).Biochemistry 16 1626–1630.
Barber, J. (1980).Biochim. Biophys. Acta 594 253–308.
Brandolin, G., Meyer, C., Defaye, G., Vignais, P. M., and Vignais, P. V. (1974).FEBS Lett. 49 149–153.
De Vendittis, E., Palumbo, G., Parlato, G., and Bocchini, V. (1981).Anal. Biochem. 115 278–286.
Douzou, P., and Maurel, P. (1977).Trends Biochem. Sci. 2 14–17.
Duszynski, J., and Wojtczak, L. (1974).FEBS Lett. 40 72–76.
Engasser, J. M., and Horwath, C. (1975).Biochem. J. 145 431–435.
Goldstein, L. (1972).Biochemistry 11 4072–4084.
Goldstein, L., Levin, Y., and Katchalski, E. (1964).Biochemistry 3 1913–1919.
Kamo, N., Muratsugu, M., Kurihara, K., and Kobatake, Y. (1976).FEBS Lett. 72 247–250.
Ligeti, E., and Fonyo, A. (1977).FEBS Lett. 79 33–36.
Maurel, P., and Douzou, P. (1976).J. Mol. Biol. 102 253–264.
Meisner, H. (1971).Biochemistry 10 3485–3491.
Meisner, H. (1973).Biochim. Biophys. Acta 318 383–389.
Michejda, J., and Vignais, P. V. (1981).FEBS lett. 132 129–132.
Morel, F., Lauquin, G., Lunardi, J., Duszynski, J., and Vignais, P. V. (1974).FEBS Lett. 39 133–138.
Quintanilha, A. T., and Packer, L. (1977a).FEBS Lett. 78 161–165.
Quintanilha, A. T., and Packer, L. (1977b).Proc. Natl. Acad. Sci. USA 74 570–574.
Remy, M. H., David, A., and Thomas, D. (1978).FEBS Lett. 88 332–336.
Ricard, J., Noat, G., Grasnier, M., and Job, D. (1981).Biochem. J. 195 3485–3491.
Thomas, J. A., Buchsbaum, R. N., Zimniak, A., and Racker, E. (1979).Biochemistry 18 2210–2218.
Toninello, A., Siliprandi, D., and Siliprandi, N. (1982).FEBS Lett. 142 63–66.
Tyler, D. P., and Gonze, J. (1976).Methods Enzymol. 10 75–77.
Vignais, P. V., and Vignais, P. M. (1972).FEBS Lett. 26 27–31.
Vignais, P. M., Chabert, J., and Vignais, P. V. (1975). InBiomembranes, Structure and Function (Gardos, G., and Szasz, I., eds.), North-Holland, Amsterdam, pp. 307–313.
Vignais, P. V. (1976).Biochim. Biophys. Acta 456 1–38.
Vignais, P. V., Lauquin, G. J. M., and Vignais, P. M. (1976). InMitochondria, Bioenergetics, Biogenesis, and Membrane Structure (Packer, L., and Gomez-Puyou, A., eds.), Academic Press, New York, pp. 109–125.
Waggoner, A. S., Wang, C. H., and Tolles, R. L. (1977).J. Membr. Biol. 33 109–140.
Wharton, C. W., Crook, E. M., and Brocklehurst, K. (1968).Eur. J. Biochem. 6 572–578.
Wojtczak, L., and Nalecz, M. J. (1979).Eur. J. Biochem. 94 99–107.
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Vignais, P.V., Michejda, J.W. & Doussiere, J. Inhibition by valinomycin of atractyloside binding to the membrane-bound ADP/ATP carrier: Counteracting effect of cations. J Bioenerg Biomembr 15, 243–256 (1983). https://doi.org/10.1007/BF00744523
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DOI: https://doi.org/10.1007/BF00744523