[Miocarditis in Patients with COVID-19 Confirmed by Immunohistochemical].

Aim      Despite the regular heart damage in patients with coronavirus pneumonia caused by SARS-Cov-2, a possibility of developing lymphocytic myocarditis as a part of COVID-19 remains unsubstantiated. The aim of this study was to demonstrate a possibility of lymphocytic myocarditis and to study its morphological features in patients with the novel coronavirus infection (COVID-19) with a severe course.Material and methods   Postmortem data were studied for 5 elderly patients (74.

[Study of the antigenic structure of human immunoglobulin lambda-chain using monoclonal antibodies].

Nine monoclonals against human Ig lambda chains were produced, 4 antibodies react with C-domain, 5--with V-domain of the lambda chain. Anti-C lambda domain antibodies recognize not less than 3 epitopes and one of them is expressed only on the isolated chain. Anti-V lambda antibodies bind both isolated lambda chain and intact IgG, IgM, IgA.

[Immunoenzyme test system with monoclonal antibodies to human IgG4 in the determination of allergen-specific antibodies in pollinosis].

ELISA for determination of allergen-specific IgG4 antibodies was developed with the help of monoclonal anti-IgG4 antibodies obtained by classic hybridoma technique. Subclass specificity of antibodies were studied in sera of 108 patients suffering from pollinosis. Antibodies of this isotype were found in the majority of patients with tree pollen allergy but not in patients with grass pollen allergy.

[Antigenic determinants of the constant region of human immunoglobin kappa-chain detected by monoclonal antibodies].

Ten different monoclonal antibody (monAB) preparations reacting with human IgL chains of the kappa type have been obtained. Nine of the monAB interacted with the kappa-chain C domain, whereas only one monAB reacted with the V domain. It has been determined that monAB against the C domain react with three different epitopes.

A new approach to studies of cell-antibody interactions using fluorescent lipid probes.

The interaction of poly- and monoclonal antibodies against the L-chain of human Ig with Burkitt lymphoma EB-3 cells was studied using a fluorescent lipid probe, anthrylvinyl-labelled sphingomyelin, incorporated into the cell plasma membrane. Binding of the antibodies to Ig receptors on the surface was shown to induce changes in the fluorescence polarization of the probe. The high sensitivity of the method allows one to detect less than 100 antibody molecules per cell.