Substitutions of cysteine residues of Escherichia coli heat-stable enterotoxin by oligonucleotide-directed mutagenesis.
The Escherichia coli 18-amino-acid, heat-stable enterotoxin STp has six cysteine residues linked intramolecularly by three disulfide bonds. These disulfide bonds are important for toxic activity, but the precise role of each bond is not clear. We substituted cysteine residues of STp in vivo by oligo...
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| Gepubliceerd in: | Infect Immun |
|---|---|
| Hoofdauteurs: | , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
American Society for Microbiology (ASM)
1987
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC260666/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3305364/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/iai.55.9.2121-2125.1987 |
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