[Specificity of antibodies to diphtheria toxin subunits in children with various forms of diphtheria infections].

In order to study the specificity of serum antibodies to separate subunits of diphtheria toxin, SDS-electrophoresis of diphtheria toxin preliminary disintegrated on the subunits via trypsin treatment was performed, followed by immunoblotting assay. 86 blood serum samples of children with diphtheria carriers of toxigenic and non-toxigenic strains of Corynebacterium diphtheriae as well as children with other infectious diseases similar to diphtheria in their clinical manifestation, and healthy ones immunized with DTP-vaccine were tested. A special computer program was written and applied for results processing and assumption.

[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.

[Minimal amino acid sequence, recognized by anibodies to the peptide GPQPPQPPQP from the proline-rich region of pertactin].

Three antiserum samples obtained from rabbits immunized by the conjugate KLH-10P (keyhole limpet hemocyanine-decapeptide GPQPPQPPQP) were used to study antigenic structure of 10P. Antigenic properties of conjugates 6P (PGPQPP) and 4P (PQPP) with ovalbumine were studied by an indirect immunoassay (ELISA). Also 4P, 6P, PQP and QPP peptides were used for a competition assay.

Analysis of antibodies that recognize the B-epitopes formed on protein antigens by glutaraldehyde treatment: an efficient method of their neutralization.

Immunochemical analysis of antigenic determinants (AD) formed on protein macromolecules by glutaraldehyde (GA) treatment with subsequent block of free aldehyde groups with glycine was performed. The structure of the epitopes was analyzed using BSA and ovalbumin (Ova) treated with GA with subsequent block of the active groups with glycine and other amino acids. The products of reaction of GA with Gly, Lys, Pro, and His were used as hapten-like antigens that mimic GA antigenic determinants (GA-AD).

[Analysis of B-epitopes formed on proteins after treatment with glutaraldehyde].

Structural analysis of the B-epitopes formed on protein macromolecules by glutaraldehyde treatment with subsequent block of free active groups by glycine was performed. Two types of antigenic determinants recognized by different antibody populations were found by protein chemistry and immunochemistry techniques. An efficient method of blocking the antibodies to the epitopes formed on proteins by glutaraldehyde was developed.