Immunological Data Discovery Index
Immunological Data Discovery Index
| authorizations: |
registration not required
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| accessURL: |
http://www.iedb.org/reference/1008282 |
| landingPage: |
http://www.iedb.org/assay/1480184 |
| type: |
Literature
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| publicationVenue: |
Mol Immunol
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| dates: |
1991
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| study type: | b cell assays |
| subject species: | Escherichia coli |
| fullName: |
M P Larvor
L Djavadi-Ohaniance
B Friguet
F Baleux
M E Goldberg
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| method: |
ELISA
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| name: |
Peptide/antibody recognition: synthetic peptides derived from the E. coli tryptophan synthase beta 2 subunit interact with high affinity with an anti-beta 2 monoclonal antibody.
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| description: |
Binding of mAb 164-2 to the epitope (Kd=7.5 nM) was almost as high as binding to the native beta2 tryptophan synthase protein (Kd = 1 nM). Removal of three N-terminal residues by trypsin abolishes antibody binding. The longer peptide, residues 271-296 (LKHGRVGIYFGMKAPMMQTEDGQIEE), has increased affinity (Kd = 2.8 nM). Measurement of the dissociation (koff = 1.6 x10^-3 sec^-1) and association (kon = 1.2 x10^5 M^-1sec^-1) rate constants of epitope binding to mAb 164-2 are compatible with a one-step reaction. The authors conclude that the epitope adopts in solution a conformation close to that of the native protein.
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| name: |
iedb
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| homePage: |
http://www.iedb.org |
