| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1003766 |
| landingPage: |
http://www.iedb.org/assay/1372791 |
| type: |
Literature
|
| publicationVenue: |
Biochem J
|
| dates: |
1996
|
| study type: | b cell assays |
| subject species: | Leishmania major |
| fullName: |
K P Soteriadou
A K Tzinia
E Panou-Pamonis
V Tsikaris
M Sakarellos-Daitsiotis
C Sakarellos
Y Papapoulou
R Matsas
|
| method: |
ELISA
|
| name: |
Antigenicity and conformational analysis of the Zn(2+)-binding sites of two Zn(2+)-metalloproteases: Leishmania gp63 and mammalian endopeptidase-24.11.
|
| description: |
Residues His4 and Glu5 of epitope (VVTHEMAHALG) are involved in antibody binding. Antibody binding was tested for multiple shorter peptides derived from the epitope. The shortest peptide capable of significant antibody binding was the pentapeptide VVTHE. However, highest binding was observed with the full-length epitope.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |