| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1009942 |
| landingPage: |
http://www.iedb.org/assay/1487535 |
| type: |
Literature
|
| publicationVenue: |
Biochemistry
|
| dates: |
1997
|
| study type: | b cell assays |
| subject species: | Escherichia coli |
| fullName: |
J Sun
J Li
N Carrasco
H R Kaback
|
| method: |
surface plasmon resonance (SPR)
|
| name: |
The last two cytoplasmic loops in the lactose permease of Escherichia coli comprise a discontinuous epitope for a monoclonal antibody.
|
| description: |
Epitope-specific mAb(s) did not bind lactose permease in dot blot. Single Cys replacement mutants E342C and R344C abolished mAb binding, establishing these two residues as primary determinant. Cysteine substitution of other epitopic residues (I283, K289, F334, K335, V343, and F345) resulted in reduced mAb binding.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |