| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1008342 |
| landingPage: |
http://www.iedb.org/assay/1584692 |
| type: |
Literature
|
| publicationVenue: |
Mol Immunol
|
| dates: |
1984
|
| study type: | b cell assays |
| subject species: | Tobacco mosaic virus (vulgare) |
| fullName: |
P R Morrow
D M Rennick
C Y Leung
E Benjamini
|
| method: |
ELISA
|
| name: |
The antibody response to a single antigenic determinant of the tobacco mosaic virus protein: analysis using monoclonal antibodies, mutant proteins and synthetic peptides.
|
| description: |
The epitope sequence is conserved in strains Vulgare and Dahlamense.
The epitope inhibited the binding of the mAb(s) to TMVP. There were dramatic differences in the mAb fine specificities. C-10 and B-2 mAbs are of isotypes IgG2a and IgG2b, respectively. Affinity constants were determined by equilibrium dialysis. The association constants for mAb C-10 using unfractionated ascitic fluid, antibodies purified by peptide-Sepharose, and antibodies purified by protein A-Sepharose were 8.6 x 10^6 L/mol, 16.8 x 10E6 L/mol, and 7.5 x 10^6 L/mol, respectively. The association constants for mAb B-2 using unfractionated ascitic fluid, antibodies purified by peptide-Sepharose, and antibodies purified by protein A-Sepharose were 2.2 x 10^6 L/mol, 1.9 x 10E6 L/mol, and 1.8 x 10^6 L/mol, respectively.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |