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. 1982 Feb;149(2):662–667. doi: 10.1128/jb.149.2.662-667.1982

Interaction of the maltose-binding protein with membrane vesicles of Escherichia coli.

G Richarme
PMCID: PMC216556  PMID: 7035435

Abstract

The interaction of the radioactively labeled purified maltose-binding protein of Escherichia coli with membrane vesicles was studied. The maltose-binding protein bound specifically to the vesicles, in the presence of maltose, on few sites. Under conditions in which a potential was imposed across the membrane, the specific binding was (i) increased, (ii) dependent on maltose, and (iii) abolished in a mutant defective in the tar gene product, one of the methyl-accepting chemotaxis proteins. At least 1,300 binding sites were present in the membrane fraction of logarithmically growing cells.

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Selected References

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