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Functional reconstitution of the partially purified aspartate‐glutamate carrier from mitochondria
Author(s) -
Krämer Reinhard
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81195-3
Subject(s) - glutamate receptor , mitochondrion , biochemistry , chemistry , liposome , phospholipid , affinity chromatography , chromatography , phosphate , membrane , enzyme , receptor
The aspartate/glutamate carrier from beef heart mitochondria has been solubilized with detergent. The transport protein was partially purified by chromatography on hydroxyapatite in the presence of dodecyl octaoxyethylene ether and high concentrations of ammonium acetate. During purification, the aspartate/ glutamate carrier was identified by functional reconstitution into egg yolk phospholipid liposomes. After hydroxyapatite chromatography the protein is 30 fold enriched in aspartate/glutamate transport activity but still contains ADP/ATP‐carrier and phosphate carrier. The reconstituted activity is specific for exchange of L‐aspartate and L‐glutamate and is similar to intact mitochondria with respect to substrate affinity and inhibitor sensitivity.