Uptake of ATP by submitochondrial particles from bovine heart was stimulated 15-fold by internal ADP. The transport was inhibited by atractyloside and bongkrekic acid. Vesicles prepared with soybean phospholipids and a protein fraction from mitochondria also catalyzed the ADP-dependent and inhibitor-sensitive uptake of ATP. This reconstituted system provides a suitable assay for the purification of the mitochondrial adenine nucleotide carrier.
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Shertzer et al. (1974) studied this question.
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