The N‐ and C‐termini of the tricarboxylate carrier are exposed to the cytoplasmic side of the inner mitochondrial membrane
Open Access
- 9 January 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 357 (3) , 297-300
- https://doi.org/10.1016/0014-5793(94)01379-f
Abstract
Polyclonal antibodies were raised in rabbits against two synthetic peptides corresponding to the N‐ and C‐terminal regions of the rat‐liver mitochondria) tricarboxylate carrier. ELISA tests performed with intact and permeabilized rat‐liver mitoplasts showed that both anti‐N‐terminal and anti‐C‐terminal antibodies bind only to the cytoplasmic surface of the inner membrane, indicating that both termini of the membrane‐bound tricarboxylate carrier are exposed to the mitochondria) intermembrane space. Furthermore, tryptic digestion of intact mitoplasts markedly decreased the binding of anti‐N‐terminal and anti‐C‐terminal antibodies to the tricarboxylate carrier. These results are consistent with an arrangement of the tricarboxylate carrier monomer into an even number of transmembrane segments, with the N‐ and C‐termini protruding toward the cytosol.Keywords
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