The monocarboxylate carrier from rat liver mitochondria

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Abstract
The monocarboxylate (pyruvate) carrier was extracted from rat liver mitochondria with Triton X‐100 in the presence of asolectin and partially purified by chromatography on HTP. The HTP eluate reconstituted in liposomes was shown to catalyze active pyruvatein/acetoacetateout, and acetoacetatein/pyruvateout counter‐exchange. Kinetic characterization of the reconstituted pyruvate carrier was achieved by an original spectrophotometric method consisting of determination of substrate release from proteoliposomes with a coupled enzymatic assay.