Partial purification and reconstitution of the tricarboxylate carrier from eel liver mitochondria.
The tricarboxylate carrier of the inner membrane of eel liver mitochondria has been solubilized with Triton X-100 and partially purified by chromatography of the mitochondrial extract on dry hydroxyapatite. The purified fraction has been reconstituted into liposomes and functionally analyzed. The reconstituted carrier protein catalyzed a 1,2,3-benzenetricarboxylate-sensitive citrate uptake in liposomes. The substrate specificity and the inhibitor sensitivity of the tricarboxylate carrier are similar to those previously determined for the same protein of mammalian mitochondria.
Zara
V
V
Dept. of Biology, University of Lecce, Italy.
Damiano
G
G
Franco
M R
MR
Siculella
L
L
Gnoni
G V
GV
D000818:Animals; D001555:Benzene Derivatives / Q000378:metabolism*; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D004524:Eels; D008081:Liposomes; D008930:Mitochondria, Liver / Q000378:metabolism*; D013379:Substrate Specificity; D014233:Tricarboxylic Acids / Q000378:metabolism*
D001555:Benzene Derivatives; D002352:Carrier Proteins; D008081:Liposomes; D014233:Tricarboxylic Acids; C020723:citrate-binding transport protein; C004288:benzene 1,2,3-tricarboxylic acid