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

The Journal of biological chemistry ·Vol. 250 ·No. 4 ·1975-02-25 ·Pages 1600-2

Lo TC, Sanwal BD

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.

MeSH Terms

Bacterial Proteins/isolation & purification,metabolism Biological Transport, Active Carboxylic Acids/pharmacology Chromatography, Affinity Dicarboxylic Acids/metabolism Edetic Acid/pharmacology Escherichia coli/drug effects,metabolism Fumarates/metabolism Kinetics Lactates/metabolism Magnesium/pharmacology Malates/metabolism Molecular Weight Receptors, Drug Solubility Structure-Activity Relationship Succinates/metabolism Sulfhydryl Reagents/pharmacology Zinc/pharmacology

Chemicals

Bacterial Proteins Carboxylic Acids Dicarboxylic Acids Fumarates Lactates Malates Receptors, Drug Succinates Sulfhydryl Reagents Edetic Acid Magnesium Zinc

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Lo T C

Sanwal B D

Article Info

Journal

The Journal of biological chemistry

Abbr.

J Biol Chem

ISSN

0021-9258

Published

1975-02-25

Pages

1600-2

Language

English

Region

United States

NLM ID

2985121R

Subset

External Links

PubMed source View journal details

Analysis Services

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

Contact

WeChat Official Account