Publications by authors named "Surovtsev V"

Objective: Men who have sex with men (MSM) have a high risk of lifelong anal cancer caused by high-risk human papillomavirus (HR HPV) infections. The aim of this study was to investigate the prevalence of anal canal HR HPV infection among men who have sex with men (MSM) with and without HIV infection in Moscow (Russia). We evaluated associations of some HIV coinfections (HSV and CMV) and HPV distribution among MSM with and without HIV infection.

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We compared phagocytic activity of macrophages of monocyte origin and Kupffer cells under the influence of M1 and M2 inducers and without activation. Cultures of monocyte-derived macrophages and Kupffer cells were characterized by intensive expression of CD68 that was not affected by activation factors. At the same time, these cultures demonstrated different dynamics of phagocytic activity.

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In the central nervous system and in the liver, the macrophage populations are represented exclusively by descendants of the hematopoietic progenitor cells of the yolk sac. The reasons for such differential distribution of macrophages are not fully understood. We found that, as can be judged by corresponding changes in the expression of CD86 and CD163 markers, the transient macrophages of monocytic lineage are more sensitive to activating stimuli.

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Background: In many clinical cases of extensive liver resection (e.g. due to malignancy), the residual portion is too small to maintain the body homeostasis.

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Aim: To investigate the influence of the umbilical cord-derived multipotent stromal cells (MSCs) on recovery of the liver after the subtotal resection, that is, removal of 80% of the organ mass, a renowned model of the small-for-size liver remnant syndrome.

Methods: The MSCs were obtained from the intervascular tissue of umbilical cords, dissected from rat fetuses, by the explant culture technique. The vital labeling of MSCs with РКН26 was carried out on the 3rd passage.

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pH-Dependence of the kinetic parameters of Micrococcus lysodeicticus cell lysis under the action of the protein hen egg lysozyme at the pH 6.9-10.0 at 25 and 37 degrees C has been investigated.

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A method for adsorption chromatography of proteins is proposed. A protein solution is passed through a cellulose column at a pH value corresponding to an isoelectric point of the protein. Depending on the charge of unwanted proteins, they either remain at the origin (if charges of protein and ion-exchanger are opposite) or are released from the column (if charges of protein and ion-exchanger coincide).

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The active site of lysostaphin is shown to contain a residue of glutamic acid. As judged by a pK value of 9.2 (with pentaglycine bridges in peptidoglycan of staphylococci as a substrate), another ionogenic residue could be the epsilon-amino group of a lysine.

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The rate of lysostaphin-catalyzed lysis of staphylococci follows the Michaelis-Menten equation at [E](0) << [S](0), i.e., the activity of the enzyme is proportional to its concentration.

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This work presents a method for purification of lysostaphin, a glycylglycine endopeptidase, from the culture liquid of S. simulans biovar staphylolyticus to homogeneity in a few steps. The method includes ultrafiltration and ion-exchange and hydrophobic chromatographies.

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Some pathogenic bacteria have been demonstrated to secrete specific IgA1-proteases, the enzymes cleaving the molecules of the first subclass of human immunoglobulin (IgA1) in the single point from the hinge with the formation of Fab- and Fc-fragments. Cleavage generally deprives immunoglobulins having defense properties and the enzymes are considered as pathogenic factors. How to determine the activity, purification, and the promises of use of IgA-proteases is described.

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A sensitive and precise method for quantifying protease and peptidase activities is suggested. N-Terminal amino groups of peptides which are formed during hydrolysis of the substrates react with trinitrobenzenesulfonic acid (TNBS), and the trinitrophenyl (TNP) derivatives are determined spectrophotometrically. Spontaneous hydrolysis of TNBS is considerably diminished on trinitrophenylation at pH 7.

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The authors investigated a procedure for isolating lysostaphine, a complex of enzymes that lyse the cells of virtually any S. aureus strains in the fermenter and large bottles. It was shown that the activity of the enzyme in the fermenter might be much higher than in the flask.

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The immunomodulating properties of highly purified staphylococcal protein A and its analog obtained by gene engineering techniques have been compared with those of commercial preparations. The comparison has shown that the differences observed in this investigation may be explained by the presence of admixtures of staphylococcal nature in commercial preparations. The preparations of highly purified staphylococcal and recombinant protein A stimulate humoral immune response and the processes of phagocytosis and do not show mitogenic activity with respect to T cells.

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A modified reagent for testing the hemolytic activity of human complement component C4 has been obtained. Reagent R4 was obtained by treatment of human blood serum pools with 0.075 M solution of hydrazine hydrate.

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Modified reagents for testing the hemolytic activity of human complement components, C3 and C5, have been obtained. These reagents were obtained by treatment of human blood serum pools with a saturated solution of KBr (reagent R3) or 2 M KSCN and denaturated yeasts (reagent R5). These reagents were found to be rich in the serum factor obtained through the use of DEAE-cellulose DE-52 and containing the active component of the complement (C4).

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Using affinity chromatography on IgG-Sepharose at pH 5.0, a new fragment capable of binding to IgG (domain E) was isolated from trypsin hydrolysate of protein A. Trypsinolysis of protein A was performed at low temperatures.

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The distribution of aromatic amino acid residues in the Clq molecule according to their microenvironment was studied by the methods of difference thermal and solvent perturbation spectroscopy, fluorescence and chemical modification. Out of the three tryptophan residues located in the globular part of A- chain one residue is completely exposed on the surface, while other two are only partially exposed to a solvent. Chemical modification of tryptophanyls significantly affects the hemolytic activity of Clq, that may evidence for the formation of immunoglobulin-binding sites with participation of A- chains as well as for the location of, at least, one of the three tryptophan residues in A- chain close to the immunoglobulin-binding site or even participation in the formation of the latter.

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The role of conformational changes in the mechanism of cryoprecipitation of human monoclonal immunoglobulin M (IgM) was studied. It was demonstrated that the variable moiety of the Fab-region of cryo-IgM has a site which comprises 5 to 6 charged amino acid residues. This site is responsible for intermolecular electrostatic interactions which lead to the formation of a precipitate with a decrease in temperature.

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The resting membrane potential of innervated and denervated rat diaphragm muscle fibres was studied at different concentrations of Cl-, K+ and Na+ in the external solution and following the furosemide treatment. The Cl- equilibrium potential (ECl) and resting potential are equal in innervated fibres while denervation shifts the ECl value in the positive direction when compared with the resting potential value. The postdenervation depolarization is delayed in furosemide-treated muscles.

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A chemical modification of carboxylic groups of monoclonal human cryoglobulin M has been studied. The modification by a chromophoric carbodiimide was accompanied by complete loss of IgM cryoprecipitating properties. The number of carboxylic groups important for biological activity was estimated by the Tsou method and found to be 2.

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The effect of the chemical modification of lysine, histidine, arginine, tyrosine, tryptophan residues and carboxylic groups on the cryoproperties of monoclonal human cryoglobulin M has been studied. The modification of 35-40 lysine residues and that of 42-45 arginine residues in the molecule of cryo-IgM has been shown to result in practically complete inhibition of the cryoprecipitation. The same effect is observed on the modification of 60 histidine residues per molecule and on modification of 50 or 51 carboxylic groups.

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Cytochrome c immobilized on cyanogen bromide-activated Sepharose 4B may be used to study photochemical reactions in chloroplasts. Chloroplast reduction of both immobilized and soluble forms of the cytochrome occurs along the exogenous and endogenous pathways which results in a weaker reduction of the immobilized protein as compared to that of the soluble one. The time of the reduced immobilized cytochrome c oxidation in the dark is two orders of magnitude greater than that of the soluble one.

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Cells of Bacillus megaterium immobilized due to incorporation into polyacrylamide gel retained their viability. They differed significantly in their enzymic activity from free cells: 20alpha- and 20beta-hydroxysteroid dehydrogenase activites were substantially decreased and they also showed the capacity to synthesize significant quantities of a new derivative and to destruct steroids. Immobolized protein fractions maintained 20alpha-hydroxysteroid dehydrogenase and 20beta-hydroxysteroid dehydrogenase activities but their specific activites were lower than those of native protein fractions.

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