S. A. Bobrovnik*, M. А. Demchenko, S. V. Komisarenko

Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine,
Department of Molecular Immunology, Kyiv;
*e-mail: s-bobrov@ukr.net

Received: 09 December 2025; Revised: 21 January 2025;
Accepted: 03 April 2026; Available on-line: April 2026

The interaction of PRIGs with various antigens differs radically from the interaction of specific antibodies and the corresponding antigen. First of all, this difference lies in the lower specificity of PRIGs, although there are other fundamental differences. For example, the binding of PRIGs and antigen is extremely dependent on the temperature at which the process occurs, whereas the binding of specific antibodies to antigen is not very dependent on temperature. There are also a number of substances, such as Tween 20, that significantly affect the binding of PRIGs to antigens, but have a much weaker effect on the binding of specific antibodies. This article is devoted to studying the degree of non-specificity of the PRIGs and antigen reaction, and the ability of serologically unrelated antigens to inhibit this interaction. According to the data presented in this article, the interaction between PRIGs and antigens is completely nonspecific.