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Affinity-chromatographic studies based on the binding-specificity of the lambda receptor of Escherichia coli.

Affinity-chromatographic studies based on the binding-specificity of the lambda receptor of Escherichia coli. Research Abstract Details 

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  • Affinity-chromatographic studies based on the binding-specificity of the lambda receptor of Escherichia coli. Abstract Text:

    t ferenciT Ferenci,

    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

    t ferenciT Ferenci,

    For similar proteins: membrane proteins: receptors, cell surface: receptors, virus research abstracts see: proteins: membrane proteins: receptors, cell surface: receptors, virus research

    PUBMED ID PMID:

    MEDLINE DATE:

    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

    FRANCE Research PublicationFRANCE Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: Ann Microbiol (Paris)

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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