Development of the myoglobin sensor based on the surface plasmon resonance.

Bioaffinic sensor based on the surface plasmon resonance (SPR) with golden layer as a transducer was developed. This sensor was applied for control of antigen-antibodies (Ag-Ab) interactions. For modification of transducer surface the spontaneously organized molecular assemblies of two types of mercaptan were formed. It was shown that the created bioaffinic sensor allowed to detect minimal concentration of antibodies, about 1 ng/ml, to the human heart myoglobin, which preliminary was immobilized on the sensitive surface. The particularities of the dynamics of protein interaction were observed. Duration of incubation with the biospecific component was no more than 5 minutes. After rupturing of specific binding it was possible to obtain initial signal again during 7-9 cycles.

[The effect of antibodies against Ca2(+)-ATPase and its hydrophobic fragment on the activity of this enzyme and on the passive transport of Ca2(+)]. / Vliianie antitel protiv Ca2(+)-ATPazy i ee gidrofobnogo fragmenta na aktivnost' étogo fermenta i passivnyi transport Ca2(+).

It is shown that both Ca(2+)-ATPase and its hydrophobic fragment are immunogenic factors. A region between hydrophobic and hydrophilic parts of Ca(2+)-ATP-ase is immunogenic. These antibodies clearly inhibit inflow and outflow of Ca2+ through a hydrophobic fragment reconstructed into liposomes and do not influence Ca(2+)-ATPase activity.

[Isolation and characteristics of immune complexes circulating in the serum of acute leukemia patients]. / Vydelenie i kharakteristika immunnykh kompleksov, tsirkuliruiushchikh v syvorotke krovi bol'nykh ostrym leikozom.

Immunoglobulin G-containing immune complexes are obtained from blood serum of patients with acute leukemia by the method which includes precipitation using polyethylene glycol-6000, Sephadex G-200 gel filtration and protein A-sepharose affinity chromatography (pH 8.5). Immunologically active antibodies and antigens of complexes are isolated by Sephadex G-200 gel chromatography under conditions of dissociation (the sodium-citrate buffer, pH 7.5, 9 M urea). The immune complexes with the antigens and antibodies isolated from them are partially characterized using disc-immunoelectrophoresis, isoelectrofocusing and immune-isoelectrofocusing.