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Identification and purification of the carnitine carrier from rat liver mitochondria.

Authors: Indiveri, C  Tonazzi, A  Palmieri, F 
Citation: Indiveri C, etal., Biochim Biophys Acta. 1990 Oct 24;1020(1):81-6.
Pubmed: (View Article at PubMed) PMID:2223786

The carnitine carrier from rat liver mitochondria, solubilized in Triton X-100 and partially purified on hydroxyapatite, was identified and completely purified by specific elution from celite in the presence of cardiolipin. On SDS-gel electrophoresis, the purified celite fraction consisted of a single band with an apparent Mr of 32,500. When reconstituted into liposomes the carnitine transport protein catalyzed an N-ethylmaleimide-sensitive carnitine/carnitine exchange. It was purified 970-fold with a recovery of 43% and a protein yield of 0.04% with respect to the mitochondrial extract. The properties of the reconstituted carrier, i.e., requirement for a countersubstrate, substrate specificity and inhibitor sensitivity, were similar to those of the carnitine transport system as characterized in intact mitochondria.


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CRRD Object Information
CRRD ID: 13440120
Created: 2017-10-24
Species: All species
Last Modified: 2017-10-24
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.