Functional reconstitution of the partially purified aspartate‐glutamate carrier from mitochondria

FEBS Letters

Krämer, Reinhard¹ 

[1] Institut für Physikalische Biochemie der Universität München, Goethestrasse 33, 8000 München 2, FRG

关键词: Aspartate/glutamate carrier;    Beef heart mitochondria;    Liposome;    Reconstitution;    Detergent;    Kinetics;    asp;    aspartate;    C x E y;    alkyl(x)-polyoxyethylene(y)-ether;    BKA;    bongkrekate;    CAT;    carboxyatractylate;    glu;    glutamate;    PalP;    pyridoxalphosphate;    Pipes;    piperazine-N;    N'-bis(2-ethanesulfonic acid);   

DOI  :  10.1016/0014-5793(84)81195-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown