CYP2C9 and VKORC1 gene polymorphism is inessential for bleeding development under conditions of oral application of anticoagulant acenocoumarol in Russian patients at high risk of thromboembolic complications.

The study included 52 patients at a high risk of thromboembolic complications, with permanent atrial fibrillation. All patients were treated with acenocoumarol for 6 months and the incidence of hemorrhages was evaluated in all of them. All patients were genotyped by CYP2C9 and VKORC1.

[CYP2C9 and VKORC1 gene polymorphism and acenocoumarol anticoagulant activity in Russian patients at high risk of thromboembolic complications].

The study included 25 patients at high risk of thromboembolic complications. All of them were treated with acenocoumarol for 6 months under control of the frequency of hemorrhage and episodes of severe hypocoagulation (a more than 3-fold rise in INR). All the patients underwent CYP2C9 and VKORC1 genotyping.

[Interferon activates DNA repair genes in UV-irradiated human cells].

Unscheduled DNA synthesis in human fibroblasts pretreated with natural and recombinant interferons was studied by scintillated radiometry. UDS was increased in fibroblasts pretreated 7 days before UV-irradiation. Newly synthesized proteins induced in cells after interferon treatment were compared with heat shock proteins.

[Mechanism of the antimutagenic effect of interferon in human fibroblasts based on induced protein analysis].

Proteins induced in human fibroblasts after treatment of some antimutagens (interferon, p-aminobenzoic acid, heating and vaccinia virus infection) were identified by means of polyacrylamide gel electrophoresis (10-15%) followed by fluorography of the gel. Influenza virus proteins (A/WSN/33) were used as markers to determine the molecular weights of the new proteins. The results obtained suggest that interferon, p-aminobenzoic acid, heating and vaccinia virus infection induced proteins with mol.

Consolidation of intramolecular disulfide bonds in influenza virus hemagglutinin as an element of intracellular maturation.

Electrophoretic behavior of influenza virus hemagglutinin during SDS electrophoresis in polyacrylamide gel is critically dependent on the life time in the infected cells and also on the conditions of sample preparation and analysis. During electrophoresis of total cell lysate proteins under nonreducing conditions the short-labeled hemagglutinin is detected as multiple bands, electrophoretic mobility of most of them being lower than that of hemagglutinin of viral particles. This heterogeneity failed to be detected during electrophoresis under reducing conditions which is indicative of the differences in the number or direction of intramolecular disulfide bonds between short-labeled and mature hemagglutinin molecules.