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Immunochemical characterization of the adenine nucleotide translocator

Immunochemical characterization of the adenine nucleotide translocator Antibodies have been prepared against purified preparations of the heart and kidney nucleotide translocator in the ‘c’‐conformation. The results show organ‐specific antigenic determinants on the translocator proteins isolated from heart, kidney and liver although a partial cross‐reactivity between these three proteins was demonstrable. The organ specificity was observed both with the solubilized and with the membrane‐bound translocator protein indicating organ‐specific determinants on exposed regions of the carrier. An organ‐specific inhibition of the nucleotide transport in heart mitochondria by the heart carboxyatractylate‐protein antiserum leads to the conclusion that the organ specificity is at least partially conditioned by the binding site for the substrate and/or the closely linked gate of the carrier protein. Apart from the organ specificity the results also demonstrate a specificity of the antibodies for the translocational conformations of the carrier: the ‘c’‐conformation stabilized in the carboxyatractylate‐protein complex and the ‘m’‐conformation present in the bongkrekate‐protein complex. However, after denaturation of the carboxytratylate‐protein and bongkrekate‐protein complexes the binding of the anti‐(carboxyatractylate‐protein) antiserum to both inhibitor‐protein complexes was nearly identical. The conformation specificity was also expressed by the inhibition of the conformation transition from the ‘c’‐ to the ‘m’‐state. This side‐specific inhibition of the nucleotide transport and the identical binding activity of the carboxyatractylate‐protein antiserum against the denatured carboxyatractylate‐protein and bongkrekate‐protein complexes suggested that the conformation‐specific antigenic determinants are topographic surface regions which are determined by the chain folding. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Febs Journal Wiley

Immunochemical characterization of the adenine nucleotide translocator

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References (27)

Publisher
Wiley
Copyright
Copyright © 1984 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1742-464X
eISSN
1742-4658
DOI
10.1111/j.1432-1033.1984.tb08412.x
Publisher site
See Article on Publisher Site

Abstract

Antibodies have been prepared against purified preparations of the heart and kidney nucleotide translocator in the ‘c’‐conformation. The results show organ‐specific antigenic determinants on the translocator proteins isolated from heart, kidney and liver although a partial cross‐reactivity between these three proteins was demonstrable. The organ specificity was observed both with the solubilized and with the membrane‐bound translocator protein indicating organ‐specific determinants on exposed regions of the carrier. An organ‐specific inhibition of the nucleotide transport in heart mitochondria by the heart carboxyatractylate‐protein antiserum leads to the conclusion that the organ specificity is at least partially conditioned by the binding site for the substrate and/or the closely linked gate of the carrier protein. Apart from the organ specificity the results also demonstrate a specificity of the antibodies for the translocational conformations of the carrier: the ‘c’‐conformation stabilized in the carboxyatractylate‐protein complex and the ‘m’‐conformation present in the bongkrekate‐protein complex. However, after denaturation of the carboxytratylate‐protein and bongkrekate‐protein complexes the binding of the anti‐(carboxyatractylate‐protein) antiserum to both inhibitor‐protein complexes was nearly identical. The conformation specificity was also expressed by the inhibition of the conformation transition from the ‘c’‐ to the ‘m’‐state. This side‐specific inhibition of the nucleotide transport and the identical binding activity of the carboxyatractylate‐protein antiserum against the denatured carboxyatractylate‐protein and bongkrekate‐protein complexes suggested that the conformation‐specific antigenic determinants are topographic surface regions which are determined by the chain folding.

Journal

The Febs Journal – Wiley

Published: Sep 1, 1984

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