[Stability of serum immunoglobulin conformation in various tumors].

As shown by means of temperature-perturbation differential spectrophotometry blood serum immunoglobulins G from patients with gastric cancer and with some other tumors were more resistant to 2 M urea as compared with the immunoglobulins from healthy volunteers and patients with gastric ulcerous disease. The resistance of IgG conformation was altered in the course of gastric cancer treatment.

[The effect of low concentrations of urea on immunoglobulin conformation from the data of differential spectrophotometry].

A reversible noncooperative conformational transition takes place in IgG molecule at 1 divided by 3 M urea solutions in the temperature interval 10 divided by 40 degrees C. This transition is registered as an increase of chromophores exposure and preceeds denaturation which happens at the same temperatures and with higher urea concentration.

[Molecular mechanisms of protective reactions of the body: time scale, specificity scale].

Heterogeneous conformation transition (HCT) peculiar to proteins is the earliest protection of the organism from poisons, toxins and pathological metabolites, HCT is conjugated with the biosynthesis of heat shock proteins (HSP), glycosylation of modified albumin and with an increase in the biosynthesis of soluble lectins, acute phase reactants (APR). All phases except for HCT are regulated at different levels of the protein biosynthesis. Their individual time corresponds to the evolution stages.

[A method of isoelectric focusing in a borate-polyol system with pH gradient of 4.0 to 5.6 in a thin layer of polyacrylamide gel].

A procedure is described for thin-layer polyacrylamide gel isoelectric focusing involving borate-polyol system with gradient pH 4.0-5.6, where 0.