[Use of ascorbic acid for raising clinical response to long-acting nitrates].

The data of clinic observation and ECG-monitoring show that ascorbic acid significantly increases antianginal vasodilatory effects of nitroglycerine thus preventing from development of ischemic miocardial reaction in response to complamin injection. Incubation under anaerobe conditions of ascorbic acid solution with NO-donors (sodium nitrate, nitroglycerine) or with the blood of ischemic patients who had been treated for a long time with long-acting nitrovasodilators, results in liberation in Varburg vasculium of gas bubbles identified as nitrogen oxide according to hemoglobin nitrosylation. Activation of endogen NO-donors with ascorbic acid and taking antilogs of antianginal effects of exogenous nitroglycerine makes it possible to substantially increase the efficiency of nitratotherapy and nitratoprophylaxis of angina pectoris.

[Study of heat denaturation of human serum albumin in water-alcohol and water-salt solutions in the presence of organic ligands].

The method of differential scanning microcalorimetry was used to show a decrease in heat stability of serum albumin in the presence of aliphatic alcohols. In aqueous-alcohol media, the melting temperature, denaturation transition enthalpy were decreased, and the protein intermolecular aggregation enhanced. When the alcohol concentration in aqueous solution was elevated, the number of epsilon-amino groups of lysine residues in human serum albumin exposed to the solvent rose from 6-7 in aqueous solution to maximum 20 groups in the aqueous-alcohol solution, respectively.

[Spectral-fluorescent characteristics of rat transcortin in normal conditions and during experimental circulatory insufficiency].

Spectral-fluorescent parameters of rat transcortin isolated from blood plasma of intact rats and rats with circulatory insufficiency were studied. The differences in the Schtern Folmer constants and the dissociation constants for the transcortin-corticosterone complex obtained during the protein titration by corticosterone may be due to different tryptophanyl surroundings in the molecules of the studied proteins. This may be a consequence of the conformational rearrangements of the corticosteroid-binding globulin molecules.