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).

The organization of potato virus X coat proteins in virus particles studied by tritium planigraphy and model building.

Potato virus X particles containing the intact, undegraded Ps form of the coat protein and particles containing the in situ degraded Pf form of the coat protein, which is devoid of 19-21 amino acids from the N-terminus, were bombarded with thermally activated tritium atoms, and the intramolecular distribution of the tritium label was studied. The tritium planigraphy revealed that the N-terminal region of the coat protein is the most accessible region for both type of PVX particles. The C-terminal region of the coat protein in the intact virus particles is almost inaccessible to the hot tritium atoms, whereas in Pf particles this region becomes available for the tritium label.