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. 1992 Dec;100(4):2030–2034. doi: 10.1104/pp.100.4.2030

Isolation and Characterization of the Tricarboxylate Transporter from Pea Mitochondria 1

Cecilia A McIntosh 1, David J Oliver 1
PMCID: PMC1075902  PMID: 16653235

Abstract

The tricarboxylate transporter was solubilized from pea (Pisum sativum) mitochondria with Triton X-114, partially purified over a hydroxylapatite column, and reconstituted in phospholipid vesicles. The proteoliposomes exchanged external [14C]citrate for internal citrate or malate but not for preloaded d,l-isocitrate. Similarly, although external malate, succinate, and citrate competed with [14C]citrate in the exchange reaction, d,l-isocitrate and phosphoenolpyruvate did not. This tricarboxylate transporter differed from the equivalent activity from animal tissues in that it did not transport isocitrate and phosphoenolpyruvate. In addition, tricarboxylate transport in isolated plant mitochondria, as well as that measured with the partially purified and reconstituted transporter, was less active than the transporter isolated from animal tissues.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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