These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Isolation of the soluble substrate recognition component of the dicarboxylate transport system of Escherichia coli.
    Author: Lo TC, Sanwal BD.
    Journal: J Biol Chem; 1975 Feb 25; 250(4):1600-2. PubMed ID: 803506.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]