Effect of substitution for arginine residues near position 146 of the A subunit of Escherichia coli heat-labile enterotoxin on the holotoxin assembly.

doi:10.1111/j.1348-0421.1995.tb02188.x

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Article

Effect of substitution for arginine residues near position 146 of the A subunit of Escherichia coli heat-labile enterotoxin on the holotoxin assembly.

Microbiology and immunology - 1 Jan 1995

Okamoto K, Takatori R, Okamoto K

Abstract excerpt

Escherichia coli heat-labile enterotoxin (LT) is a holotoxin which consists of one A and five B subunits. Although B subunit monomers released into periplasm can associate into pentameric structures in the absence of the A subunit, the A subunit accelerates the assembly. To express the function, A subunit constructs the proper spatial structure. However, the regions involved in the construction are unknown. To...

Topics

Amino Acid Sequence
Animals
Antibodies, Bacterial
Arginine
Bacterial Toxins
Base Sequence
DNA Primers
Electrophoresis, Polyacrylamide Gel
Enterotoxins
Enzyme-Linked Immunosorbent Assay
Epitopes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Escherichia coli

Escherichia coli Proteins

Glycine

Immunodiffusion

Molecular Sequence Data

Mutagenesis, Site-Directed

Mutation

Source

Open in PubMed

Identifiers

PMID: 7541507
DOI: 10.1111/j.1348-0421.1995.tb02188.x

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7541507-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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