[A non-invasive method of evaluation of Helicobacter pylori urease activity: its perfection and introduction to clinical practice].

The authors have developed a highly sensitive method of non-invasive diagnostics of Helicobacter pylori, the most frequent human infection. Detection of urease activity is based upon measurement of the degree of the elevation of stable 13C isotope content in exhaled air after administration of C-urea as a test reagent. The method has been scarcely applied in Russia because the test preparation, 13C urea had not been produced domestically until 2002.

[A comparative study of the effect of pyrazole on the activity of enzymes in the alcohol/polyol dehydrogenase family].

A comparative study of the effect of pyrazol, an inhibitor of the coenzyme-binding site of alcohol dehydrogenases, on the activity of enzymes of the alcohol/polyol dehydrogenase group has been carried out. Commercial preparations of alcohol dehydrogenases from the cytoplasm of horse liver cells and yeast cells, as well as the enzyme from the cytoplasm of Trichosporon pullulans cells was completely inhibited by 1 mM pyrazol, while alcohol dehydrogenases from Candida utilis and Saccharomyces carlsbergensis were inhibited only by 25% and the enzymes from Saccharomyces cerevisiae and Torulopsis candida by 30 and 38%, respectively. The inhibition degree of alcohol dehydrogenases from the cytoplasm of liver cells of various mammals (bull, calf, rat, gopher) and birds (hen, pheasant, duck) varied from 12 to 42% in the presence of 1 mM pyrazol.

[The possible effect of amino acids forming a loop in the surface layer of subunits on the electrophoretic mobility of enzymes in the alcohol/polyol dehydrogenase family].

Relative electrophoretic mobility (REM) of alcohol dehydrogenases from equine hepatocyte cytoplasm was low probably due to the presence of a loop which consisted of 21 amino acid residues in the surface layer of the enzyme subunits. The REM of multiple molecular forms of alcohol dehydrogenases from yeast cell cytoplasm was higher as consistent with the absence of this loop in the surface layer of the enzyme subunits. Possible role of amino acid residues comprising the loop, in the formation of total charge and their effect on REM values of enzymes from the alcohol/polyol dehydrogenase family are discussed.

[The effect of superoxide dismutase on histochemical detection of dehydrogenases on zymograms using sorbitol dehydrogenase as an example].

Sorbitol dehydrogenases from the cytoplasm of plant, animal, and microbial cells was used to study the effect of superoxide dismutase on histochemical exposure of dehydrogenases after their electrophoretic separation. In some organisms, both enzymes are localized in the same region, which finally leads to the formation of hydrasine tetrazolium, a soluble colourless compound, but not of diformazan, an insoluble stained derivative of tetrazolium nitroblue. The experimental conditions for histochemical exposure of the enzymes in gels are discussed.

[Activity of alcohol dehydrogenase from cell cytoplasm of several types of yeast].

The author studied the activity of alcohol dehydrogenase from the cytoplasm of Saccharomyces cerevisiae, Saccharomyces carlsbergensis, Candida utilis and Torulopsis candida cells. The "classical" alcohol dehydrogenase and the octanol dehydrogenase from the T. candida cytoplasm are active in a wide range of pH from 7.