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Identification and purification of the aspartate/glutamate carrier from bovine heart mitochondria

Biochimica et Biophysica Acta (BBA) - Biomembranes, ISSN: 0005-2736, Vol: 1106, Issue: 2, Page: 291-296
1992
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The aspartate/glutamate carrier from bovine heart mitochondria was solubilized with dodecyl-octaoxyethylene ether (C 12 E 8 ) and purified by chromatography on hydroxyapatite and celite. On SDS gel electrophoresis, the purified aspartate/glutamate carrier consisted of a single protein band with an apparent M r of 31 500. When reconstituted into lipososomes the aspartate/glutamate carrier protein catalyzed an N -ethylmaleimide-sensitive aspartate/aspartate exchange. It was purified 620-fold with a recovery of 17.2% and a protein yield of 0.03% with respect to the mitochondrial extract. The properties of the reconstituted carrier, i.e. requirement for a counteranion, substrate specificity and inhibitor sensitivity, were similar to those of the aspartate/glutamate carrier as characterized in mitochondria.

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