Reference : The N- and C-termini of the tricarboxylate carrier are exposed to the cytoplasmic sid...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/32807
The N- and C-termini of the tricarboxylate carrier are exposed to the cytoplasmic side of the inner mitochondrial membrane.
English
Capobianco, L. [ > > ]
Bisaccia, F. [ > > ]
Michel, A. [ > > ]
Sluse, Francis mailto [Université de Liège - ULg > Département des sciences de la vie > Bioénergétique et physiologie cellulaire >]
Palmieri, F. [ > > ]
1995
FEBS Letters
Elsevier Science
357
297-300
Yes (verified by ORBi)
0014-5793
Amsterdam
The Netherlands
[en] Tricarboxylate carrier ; N-terminus ; C-terminus ; Antibodies ; trypsin digestion ; Mitochondria
[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.
http://hdl.handle.net/2268/32807

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