| Autor: |
Skok MV; Palladin Institute of Biochemistry, NAS of Ukraine, Kyiv. skok@biochem.kiev.ua, Lykhmus OY, Bobrovnik SO, Solodova OV, Tzartos SJ, Tsouloufis T, Vanderesse R, Marraud M |
| Jazyk: |
angličtina |
| Zdroj: |
Ukrains'kyi biokhimichnyi zhurnal (1999 ) [Ukr Biokhim Zh (1999)] 2002 Jul-Aug; Vol. 74 (4), pp. 54-60. |
| Abstrakt: |
The antibodies to nicotinic acetylcholine receptor alpha(181-192) synthetic peptides were elicited in rabbits and mice using the peptides conjugated to protein carriers in different orientations, either through C-terminal Cys (S-conjugates), or through amino groups (N-conjugates). S-conjugated peptides were less potent in eliciting peptide-specific antibodies compared to N-conjugates and this type of conjugation resulted in antibodies to the coupling reagent. However, the epitopes present in either S- or N-conjugated peptides appeared to be similar, indicating that amino acid residues, which form the epitope, were located in the middle part of the peptide and did not include both N- and C-terminal residues. Peptide conjugation to a protein carrier did not play a role in stabilizing the peptide conformation, but was necessary to concentrate the peptide epitopes on the carrier surface enabling bivalent antibody binding. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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