[Antigenic properties of glycine residue blocking aldehyde groups of cross-linking agent in peptide-protein conjugates].

Glutaraldehyde treatment of proteins and blocking free aldehyde groups by amines results in appearance of the antigen determinants, which include into their structure the residues both of glutaraldehyde and blocking agent (usually, glycine). The glycine-specific antibodies were detected and then selected by the immunosorbent glycine-oxyran-Sepharose. These antibodies have recognized glycine conjugated with proteins by glutaraldehyde and glycine conjugated with glycogen by bis-oxyran, however they have failed to recognized others amino acids in the analogical conjugates. It is assumed that glycine residue is a immunodominant group in the structure of epitope, which is recognized by these antibodies. Authors suppose that the proteins after the glutaraldehyde treatment can be used for obtaining the antibodies with high specificity to amino acids or other amines.