Publications by authors named "Zharmukhamedova T"

For evaluation of the effect of high-fat diet on the development of diabetic complications, the rats were maintained on standard or high-fat diet. In 3 weeks, diabetes mellitus was modeled by single intraperitoneal injection of streptozotocin. Changes in hematological parameters, physical and biochemical parameters of the urine, and in the development of thermal allodynia were different after 15-week standard and high-fat diets.

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The creation of effective bioscavengers as a pretreatment for exposure to nerve agents is a challenging medical objective. We report a recombinant method using chemical polysialylation to generate bioscavengers stable in the bloodstream. Development of a CHO-based expression system using genes encoding human butyrylcholinesterase and a proline-rich peptide under elongation factor promoter control resulted in self-assembling, active enzyme multimers.

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The protective effects of 70-kDa heat shock proteins (HSP70) were studied following the intravenous administration in rats with endotoxic shock. The antitoxic effects of both bovine HSP70 (bHSP70) and human recombinant HSP70 (hrHSP70) were compared. The preventive uptake of HSP70 decreased the toxic influence of the E.

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To determine whether primary fibroblasts producing latent transforming growth factor beta1 (TGF-beta1) are capable of down-regulating experimental autoimmune encephalomyelitis (EAE), a retroviral vector TGF-beta1-pBabe-neo (-5'UTR) was used for efficient gene transfer into primary skin fibroblasts of DA rats. After heat activation, conditioned medium from the transduced fibroblasts was found to inhibit significantly in vitro proliferation of lymphocytes from lymph nodes of DA rats with EAE. Intraperitoneal administration of TGF-beta1-transduced fibroblasts into DA rats during the priming phase of EAE resulted in a significant reduction in mortality and in the mean clinical and EAE scores versus the control immunized animals treated with non-transduced fibroblasts.

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We have synthesized two peptides, VKGFY and cyclo(VKGFY) (referred to as pentarphin (PNT) and cyclopentarphin (cPNT), respectively), and found that both peptides at 1 nM concentration increased the adhesion and spreading of murine peritoneal macrophages as well as their bactericidal activity in vitro, as shown by phagocytosis of Salmonella typhimurium virulent strain 415. PNT administered intraperitoneally at dose 20 microg/mouse on day 7, 3, and 1 prior to the isolation of macrophages also enhanced the macrophage adhesion and spreading. The receptor binding characteristics of PNT and cPNT were examined using 125I-labeled PNT.

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A strain producing the site-specific endonuclease BspF4I was found during screening of thermophilic bacteria isolated from soil. The restriction endonuclease, free from contaminant nonspecific nucleases, was purified using three steps of column chromatography--on hydroxyapatite, blue agarose, and DEAE-Trisacryl. The enzyme is stable on storage and exhibits maximal activity at 48-56 degrees C in the presence of albumin in buffer containing 10 mM Tris-HCl (pH 7.

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The effect of sugar and its phosphate derivatives on sorbitoldehydrogenase from bovine liver has been studied. The presence of 100 mM glucose, mannose, and arabinose did not influence that activity of the studied reaction, whereas fructose, sorbose, and xylose, inhibit the reaction by 20-25%. This can be explained in terms of inhibition by the final reaction products.

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The kinetic properties of sorbitol dehydrogenase from calf liver cell cytoplasm during sorbitol oxidation were studied at pH 7.0, 7.5, 8.

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A comparative study of sorbitol dehydrogenase activity in bovine, calf, and rat liver cell cytoplasm has been carried out. The level of activity of the enzyme is several times greater than that of marker enzymes (alcohol dehydrogenase, glucose-6-phosphate dehydrogenase). The data obtained suggest that the polyol (sorbitol) metabolism pathway of glucose functions actively in mammalian liver cells.

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Partially purified preparation of sorbitol dehydrogenase, isolated from hepatocytes of bovine liver tissue, was active at a wide range of pH exhibiting the maximal activity at pH 9.0 in presence of NAD but not of NADP. The high rate of sorbitol and xylitol dehydration was observed, whereas the enzyme dehydrated ribitol at the 4-fold lower rate.

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