Kinetic parameters of polyreactive immunoglobulins interaction with antigens in the presence of protamine.

The discovered earlier phenomenon of the enhancment of polyreactive immunoglobulines (PRIGs) binding to antigens in the presence of protamine and Tween 20 was investigated in more details. The comparative analysis of PRIGs reaction dynamics with immobilized antigen was provided. In addition, the rate constants for the reaction and the affinity constants of PRIGs-antigen binding in the presence or absence of optimal protamine concentration were determined.

FUNDAMENTAL DIFFERENCES BETWEEN NATURAL ANTIBODIES AND POLYREACTIVE IMMUNOGLOBULINS.

A problem of similarity and differences between so-called polyreactive immunoglobulins (PRIGs) and natural antibodies (NAbs), capable of cross-reacting with some structurally dissimilar antigens, has been considered. The analysis of mechanisms of an unspecific interaction between PRIGs or NAbs and antigens evidences for the fact that essential differences exist between these substances. These differences permit classifying the abovementioned substances as different types of immunoglobulin molecules.

[BIOLOGICAL AND IMMUNOCHEMICAL PROPERTIES OF POLYREACTIVE IMMUNOGLOBULINS].

A previously unknown phenomenon of acquired polyreactivity for serum immunoglobulins, which were subjected either to solutions of KSCN (3.0-5.0 M), low/high pH (pH 2.

Age changes of human serum polyreactive immunoglobulins (PRIG) activity.

It has been determined that activity of serum polyreactive immunoglobulins (PRIG) changes with age in practically healthy people at the age from twenty five to seventy. Therewith, the activity of serum IgG PRIG increases most of all (about 3-4 times), while IgM PRIG activity, on the contrary, does not increase, but sometimes even decreases with age. IgA PRIG activity varies significantly more than IgG PRIG activity and, besides, IgA PRIG significantly less depends on age than IgG PRIG.

[Interaction peculiarities of polyreactive immunoglobulins and various antigens].

The influence of twin 20, lysozyme and protamine on the capability of polyreactive immunoglobulins (PRIG) to attach to various antigens was investigated. Twin 20 can inhibit the binding of PRIG to antigens on immunological plates but lysozyme and protamine can enhance it. As far as the mixture of the optimal concentrations of lysozyme and protamine cannot increase PRIG-antigen interaction in comparison to the optimal dose of protamine, we have concluded that the mechanism of their effect on PRIG binding is similar.