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Lo, T.C. et al.

Isolation of the soluble substrate recognition component of the dicarboxylate transport system of Escherichia coli.

A soluble, periplasmic protein was isolated from Escherichia coli cells by chromatography on columns of aspartate-coupled Sepharose 4B. This protein has a molecular weight of about 15,000 and, as judged by competition experiments, binds the three dicarboxylic acids, succinate, malate, and fumarate and, addition, the monocarboxylic acid D-lactate. The periplasmic protein seems to be missing from some mutants of E. coli (designated cbt) which are incapable of transporting succinate in whole cells.[1]

References

Isolation of the soluble substrate recognition component of the dicarboxylate transport system of Escherichia coli. Lo, T.C., Sanwal, B.D. J. Biol. Chem. (1975) [Pubmed]

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