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The monocarboxylate carrier from rat liver mitochondria. Purification and kinetic characterization in a reconstituted
F Capuano1, M Di Paola, A Azzi
1Institute of Medical Biochemistry and Chemistry, University of Bari, Italy.
FEBS Letters
|February 12, 1990
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.