Monoclonal anti-gonadotropin releasing hormone (GnRH) antibodies reacting to sequence of GnRH preferentially recognize to native hormone.
Indian J Exp Biol
;
1989 Jan; 27(1): 1-4
Article
Dans Anglais
| IMSEAR
| ID: sea-56286
ABSTRACT
Monoclonal anti-GnRH antibodies (MoAbs) P862, P778, P813 and P764 reacted optimally to native GnRH and poorly to GnRH(OH) of sequence 4-6, 7-10, 4-10 and 1-10. The heptapeptide 4-10 showed maximum reactivity amongst the four peptides tested for immunoreactivity. Sepharose 4B-GnRH(OH)4-10 (H-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-OH) column was therefore used to purify the fraction of MoAb reacting to this sequence. The affinity purified MoAbs (A-MoAbs) were further characterized for their binding to the different sequences and affinity with native GnRH. The binding, cross-reactivity and affinity characteristics of A-MoAbs were comparable with those of MoAbs. Immunoreactivity of A-MoAbs was also observed to be partly regained when GnRH(OH)1-10 was coupled to Lys, Lys-MDP or H-Ala-Ala-Thr-Lys-Pro-Arg-OH. These observations clearly demonstrate that MoAbs were neither contaminated nor were sequence specific but were directed against the conformation of the molecule.
Texte intégral:
Disponible
Indice:
IMSEAR (Asie du Sud-Est)
Sujet Principal:
Fixation compétitive
/
Chromatographie d'affinité
/
Hormones hypophysiotropes libératrices
/
Animaux
/
Conformation moléculaire
/
Anticorps monoclonaux
/
Affinité des anticorps
langue:
Anglais
Texte intégral:
Indian J Exp Biol
Année:
1989
Type:
Article
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