A. V. Morozova

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The proteinase previously described as an unidentified component of E. coli A2 extracts which hydrolyses actin at a new cleavage site (Khaitlina et al. (1991) FEBS Lett. 279, 49) was isolated and further characterized. A chromatographic method of proteinase purification was developed by which a purity of more than 80% was attained. The enzyme was identified(More)
It has been found that actin-specific bacterial protease ECP32 cleaves prokaryotic heat shock protein DnaK, which belongs to the family of heat shock proteins with molecular weight 70 kDa. We propose a new one-step method for DnaK purification using heat treatment. The technique yields ~1 mg of partially purified DnaK from 25 g of wet bacterial biomass.(More)
Induced pluripotent stem (iPS) cells are derived from somatic cells reprogrammed to the pluripotent state by the induced expression of defined transcription factors, achieved for the first time by the seminal work of Takahashi and Yamanaka. This new type of pluripotent cells has offered new exciting options in regenerative medicine allowing the replacement(More)
We measured by the immunoenzyme assay serum levels of total IgE and leptin in 17 men and 95 women with non-alcoholic fatty liver diseases (NAFLD) and in 57 men and 25 women with alcoholic liver disease (ALD) in comparison with 454 control men and 74 women without hepatic pathology. It was shown that the total serum IgE level in patients with ALD (229.5 +/-(More)
The protease ECP32 is significant in investigations of actin, the basic protein of muscles and the cytoskeleton. The enzyme originates from the natural enterobacteria strain, which accumulates minor amounts of the protease intracellularly at the post-exponential growth phase. The limiting factor for biosynthesis is the amount of oxygen that has entered the(More)
A procedure for isolation of bacterial protease ECP32 yielding 100 microg of the enzyme from 10 liters of the Escherichia coli strain A2 liquid culture has been developed. The procedure includes chromatography, ultrafiltration, and PAGE under non-denaturing conditions. The purified preparation contained about 80% ECP32 and did not exhibit ATPase activity.(More)