Characterization, purification and properties of the yeast mitochondrial dicarboxylate carrier (Saccharomyces cerevisiae).

The dicarboxylate carrier has been characterized and purified from mitochondria of wild strain Saccharomyces cerevisiae. The mitochondria were solubilized with Triton X-100 and the detergent extract was chromatographed on hydroxylapatite. SDS-PAGE of the hydroxylapatite pass-through showed five protein bands with M(r)s ranging from 28,000 to 35,000, by silver nitrate staining.

Purification of the rat-liver mitochondrial dicarboxylate carrier by affinity chromatography on immobilized malate dehydrogenase.

The dicarboxylate carrier of rat-liver mitochondria, extracted by Triton X-100 and partially purified by hydroxylapatite chromatography, was retained by malate dehydrogenase immobilized on Sepharose gel, and eluted with 0.4 M NaCl. SDS-polyacrylamide gel electrophoresis of the eluate showed a predominant peptide band with an M(r) of 28,000.