[THE QUANTIFICATION OF SULPHATED GLYCOSAMINOGLYCANS IN RAT URINE IN EXPERIMENTAL HEMORRHAGIC CYSTITIS].

The paper presents the study of the excretion of sulfated glycosaminoglycans (GAG) in the urine of rats in experimental hemorrhagic cystitis induced by cyclophosphamide and treated with glycosaminoglycan replacement therapy. Rats were given intraperitoneal injections of cyclophosphamide at a dose of 100 mg per 1 kg body weight and subsequently treated with intragastric administration of the combined preparation of glycosaminoglycans containing glucosamine hydrochloride and chondroitin sulfate at a dose of 10 and 100 mg per 1 kg of body weight. Within 24 or 72 hours after cystitis induction there was a statistically significant increase in urinary GAG excretion. The study also found a decrease (from 1.34 to 1.22 mg/dL) in urinary GAG within 0 to 72 hours following induction of acute cystitis without glycosaminoglycan therapy. In the subchronic model of inflammation in the bladder, upon repeated administration of low doses of cyclophosphamide (50 mg/kg), decrease in urinary GAG within 0 to 72 hours (1,32±0,13 mg/dL) as well as increased excretion after 96 hours at a concentration of 2,29±0,13 mg/L after initiation cystitis were found.

[On necessity to modify biochemical methods for detecting organophosphorus componds in chemical weapons extinction objects (review of literature)].

The article covers problems of biochemical methods assessing organophosphorus toxic compounds in objects of chemical weapons extinction. The authors present results of works developing new, more specific and selective biochemical methods.

[Serum albumin: search for new sites with esterase activity according to molecular modeling data].

It is known that albumin is able to cut ester bonds in organophosphates (OPs). Amino acids responsible for esterase and pseudo-esterase activity of albumin towards OPs are still not determined. The purpose of this study is to identify the potential sites of esterase activity of albumin by the example of its interaction with soman using molecular modeling methods. The structures of the protein complexes with soman was determined by molecular docking procedure, the stability of the complexes were simulated using molecular dynamics method. It has been determined that productive sorption of soman near Tyr411 is possible only after deprotonation of the tyrosine. Tyr150 binds soman more efficiently than Tyr411; deprotonation of Tyr150 does not affect the binding efficiency, but affects on the stability of the complexes. The true esterase activity of albumin Tyr150 in relation to soman is proposed. It is shown that Ser193 can also be responsible for the esterase activity of albumin. We hypothesize that deprotonation of catalytic amino acid in one of the sites could be initiated by ligand binding in other sites (allosteric regulation).