Facilitated diffusion of p-nitrophenyl-alpha-D-maltohexaoside through the outer membrane of Escherichia coli. Characterization of LamB as a specific and saturable channel for maltooligosaccharides.-Reference-Cited by-同舟云学术

Facilitated diffusion of p-nitrophenyl-alpha-D-maltohexaoside through the outer membrane of Escherichia coli. Characterization of LamB as a specific and saturable channel for maltooligosaccharides.

Published:1988-01 Issue:1 Volume:263 Page:314-320
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Freundlieb S,Ehmann U,Boos W

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference46 articles.

1. Isolation of the Bacteriophage Lambda Receptor from Escherichia coli

2. Interaction of bacteriophage K10 with its receptor, the lamB protein of Escherichia coli

3. Mutations affecting antigenic determinants of an outer membrane protein of Escherichia coli.

4. malB Region in Escherichia coli K-12: Characterization of New Mutations

5. Structure of the malB region in Escherichia coli K12

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