| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1000873 |
| landingPage: |
http://www.iedb.org/assay/1268163 |
| type: |
Literature
|
| publicationVenue: |
Biochemistry
|
| dates: |
1990
|
| study type: | b cell assays |
| subject species: | Vibrio cholerae |
| fullName: |
J Anglister
B Zilber
|
| method: |
nuclear magnetic resonance (NMR)
|
| name: |
Antibodies against a peptide of cholera toxin differing in cross-reactivity with the toxin differ in their specific interactions with the peptide as observed by 1H NMR spectroscopy.
|
| description: |
The interactions between the aromatic residues of the monoclonal antibody TE34, and its peptide antigen were studied by 2D TRNOE difference spectroscopy. The monoclonal antibody was previously shown not to bind to cholera toxin. According to the authors, the replacement of the peptide C-terminal carboxyl by an amide bond when the peptide sequence is part of cholera toxin is probably one of the major reasons for the lack of cross-reactivity between TE34 and the native toxin.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |