The identification of two peptide sequences of light subunits of the Lathyrus ochrus isolectins containing a sequential epitope.
A series of overlapping heptapeptides representing the entire amino acid sequences of the light subunits of the two Lathyrus ochrus isolectins were synthesized, coupled to carrier proteins, and the conjugates were reacted with polyclonal antibodies directed against the whole isolectins. Ten conjugates corresponding to two linear peptides localized respectively to the N- and C-terminal ends, reacted significantly with the polyclonal antibodies. The localization of two continuous epitopes at both ends of the chains is consistent with the regions of the chains predicted as putative antigenic determinants, according to their hydrophilicity, accessibility and flexibility.
Lueken
K
K
Laboratoire de Biologie Cellulaire, Faculté des Sciences Pharmaceutiques, Université Paul Sabatier, Toulouse, France.
Mazarguil
H
H
Rougé
P
P
D000595:Amino Acid Sequence; D000939:Epitopes / Q000302:isolation & purification; D007887:Fabaceae / Q000276:immunology; D037102:Lectins / Q000276:immunology* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000276:immunology* / Q000302:isolation & purification; D037121:Plant Lectins; D010946:Plants, Medicinal
D000939:Epitopes; D037102:Lectins; D009842:Oligopeptides; D037121:Plant Lectins