The lambda receptor in the outer-membrane of Escherichia coli is capable of binding macromolecular polysaccharides. Bio-specific binding of bacteria to covalently immobilized ligands of the lambda receptor can also be demonstrated. This finding can be exploited for the affinity-chromatographic separation of E. coli populations differing in surface-receptor characteristics. The technique is applicable to the affinity-chromatographic enrichments of mutants with changes in the lambda receptor-binding site or in the regulation of its synthesis.
Affinity-chromatographic studies based on the binding-specificity of the lambda receptor of Escherichia coli. Publishing Authors By Initials
Affinity-chromatographic studies based on the binding-specificity of the lambda receptor of Escherichia coli. Journal Published:
PUBLICATION TYPE: Research Support, Non-U.S. Gov
Journal: Annales de microbiologie
VOLUME: 133A
Page Numbers: 167-9
Journal Abbreviation: Ann. Microbiol. (Paris)
ISSN: 0300-5410
DAY: 27
MONTH: Jan
YEAR: 1982
Affinity-chromatographic studies based on the binding-specificity of the lambda receptor of Escherichia coli. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 354704
Affinity-chromatographic studies based on the binding-specificity of the lambda receptor of Escherichia coli. Keywords Mesh Terms:
KEYWORDS: Receptors, Virus
MESH TERMS: metabolism
Chemical & Substance for Abstract: Affinity-chromatographic studies based on the binding-specificity of the lambda receptor of Escherichia coli. Information
Substance Name: Amylopectin
Registry Number: 9037-22-3
Grant and Affiliation Information for Affinity-chromatographic studies based on the binding-specificity of the lambda receptor of Escherichia coli.
AFFILIATION:
Country: FRANCE
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MEDLINETA: Ann Microbiol (Paris)
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