[en] Polyclonal antibodies were raised in rabbits against two synthetic peptides corresponding to the N- and C-terminal regions of the rat-liver mitochondrial 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 mitochondrial 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Capobianco, L.
Bisaccia, F.
Michel, A.
Sluse, Francis ; Université de Liège - ULiège > Département des sciences de la vie > Bioénergétique et physiologie cellulaire
Palmieri, F.
Language :
English
Title :
The N- and C-termini of the tricarboxylate carrier are exposed to the cytoplasmic side of the inner mitochondrial membrane.
Robinson, Williams, Halperin, Leznoff J. Biol. Chem. 1971, 246:5280-5286.
Palmieri, Stipani, Quagliariello, Klingenberg (1972) Kinetic Study of the Tricarboxylate Carrier in Rat Liver Mitochondria. European Journal of Biochemistry 26:587-594.