Electrochemical gradient induced displacement of the natural ATPase inhibitor protein from mitochondrial ATPase as detected by antibodies against the inhibitor protein
Por:
Dreyfus G., Gómez-Puyou A., Tuena de Gómez-Puyou M.
Publicada:
1 ene 1981
Resumen:
Antibodies against the natural ATPase inhibitor protein of bovine heart mitochondria (1) block the inhibitory action of the protein on ATP hydrolysis by soluble or particulate F1-ATPase. By immunodiffusion tests, inhibitor protein may be detected in Mg-ATP and State 3 submitochondrial particles. The binding of 121I-labeled antibodies to submitochondrial particles that possess their ATPase in the inhibited state is several times lower than in particles that had been exposed to electrochemical gradients and which show higher rates of ATPase activity. The results indicate that electrochemical gradients induce a change in position of the inhibitor protein in relation to F1-ATPase which results in the appearance of the catalytic properties of the enzyme. © 1981 Academic Press, Inc.
Filiaciones:
Dreyfus G.:
Centro de Investigación y de Estudios Avanzados, Apartado Postal 14-740 México, D.F., Mexico
Gómez-Puyou A.:
Centro de Investigaciones en Fisiología Cellular, Universidad Nacional Autónoma de México, Apartado Postal 70-600, México, D.F., Mexico
Tuena de Gómez-Puyou M.:
Centro de Investigación y de Estudios Avanzados, Apartado Postal 14-740 México, D.F., Mexico
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