Purification and functional characterization of mutant LamB proteins.

Purification and functional characterization of mutant LamB proteins. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Purification and functional characterization of mutant LamB proteins. Abstract Text:

M Luckey,H Nikaido,

The phage lambda receptor, or LamB, proteins have been purified from several missense lamB mutants, and the properties of the channel produced by these proteins were investigated in a reconstituted liposome system. In at least one mutant, a significant reduction in the sugar selectivity of the channel was observed, and another mutant protein interacted poorly with the maltose-binding protein immobilized on Sepharose beads.

Purification and functional characterization of mutant LamB proteins. Publishing Authors By Initials

M Luckey,H Nikaido,

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:

Purification and functional characterization of mutant LamB proteins. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Annales de microbiologie

VOLUME: 133A

Page Numbers: 165-6

Journal Abbreviation: Ann. Microbiol. (Paris)

ISSN: 0300-5410

DAY: 27

MONTH: Jan

YEAR: 1982

Purification and functional characterization of mutant LamB proteins. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 354704

Purification and functional characterization of mutant LamB proteins. Keywords Mesh Terms:

KEYWORDS: Receptors, Virus

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Purification and functional characterization of mutant LamB proteins. Information

Substance Name: maltoporins

Registry Number: 0

Grant and Affiliation Information for Purification and functional characterization of mutant LamB proteins.

AFFILIATION:

Country: FRANCE

AGENCY: United States NIAID

GRANT: AI-09644

ACRONYM: AI

MEDLINETA: Ann Microbiol (Paris)

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Purification and functional characterization of mutant LamB proteins Related Publications

• Bacteriophage lambda receptor protein in Escherichia coli K-12: lowered affinity of some mutant proteins for maltose-binding protein in vitro.
• Bile salts and fatty acids induce the expression of Escherichia coli AcrAB multidrug efflux pump through their interaction with Rob regulatory protein.
• Diffusion of solutes through channels produced by phage lambda receptor protein of Escherichia coli: inhibition by higher oligosaccharides of maltose series.
• ISOLATION OF URIDINE DIPHOSPHOGALACTOSE FROM ESCHERICHIA COLI MUTANT CELLS.
• Journal of bacteriology
• PhoPQ-mediated regulation produces a more robust permeability barrier in the outer membrane of Salmonella enterica serovar typhimurium.
• Physical interaction between the phage lambda receptor protein and the carrier-immobilized maltose-binding protein of Escherichia coli.
• Proteins forming large channels from bacterial and mitochondrial outer membranes: porins and phage lambda receptor protein.
• Purification and functional characterization of mutant LamB proteins.
• Site-directed disulfide cross-linking shows that cleft flexibility in the periplasmic domain is needed for the multidrug efflux pump AcrB of Escherichia coli.
• The potential of amniotic membrane/amnion-derived cells for regeneration of various tissues.
• X-ray diffraction studies of outer membranes of Salmonella typhimurium.