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1.
Article in Russian | MEDLINE | ID: mdl-22693805

ABSTRACT

AIM: Isolation of Vibrio eltor exopolysaccharide and study of its immunochemical properties. MATERIALS AND METHODS: Rugose variants of strains V. eltor 18895 and V. eltor 18843 obtained by us by selection in M9 medium were used in the study. Exopolysaccharides (EPS) were isolated by K. Kierek (2003), S.P. Zadnova (2004), N.P. Elinova (1984) methods and analyzed for carbohydrate, protein, nucleic acid content and lipopolysaccharide impurity. EPS, LPS, R-LPS structure was compared by high-pressure chromatography. Neutral sugars and amino sugars were identified by thin layer chromatography. Polyclonal antibodies were produced against EPS preparation isolated by N.P. Elinova (1984) method. Specific activity of obtained mice sera was tested by DIA method. RESULTS: EPS isolated by N.P. Elinova method (1984) was shown not to contain extraneous impurities. V. eltor EPS structure differs from LPS and R-LPS. Monosaccharide composition of EPS from ctx+ V. eltor 18895 strain is presented by a wider specter of carbohydrates including glucose, mannose, rhamnose, galacturonic acid. Use in DIA of specific sera produced against EPS from toxigenic strain did not reveal general epitopes with capsule polysaccharides of V. cholerae O139, V. parahaemolyticus and V. vulnificus. CONCLUSION: Use of EPS as an immunogen promoted production of sera that are specific against EPS and rugose variants of Vibrio cholerae eltor that can be used for their detection or characterization.


Subject(s)
Lipopolysaccharides/chemistry , Lipopolysaccharides/immunology , Lipopolysaccharides/isolation & purification , Vibrio/chemistry , Carbohydrate Conformation , Vibrio/immunology
2.
Article in Russian | MEDLINE | ID: mdl-20468095

ABSTRACT

AIM: Determination of serogroup and PCR-genotyping of Vibrio cholerae non-O1/non-O139 strains isolated from surface basins and sewages of Rostov-on-Don city in 2003 - 2008. MATERIALS AND METHODS: Seven hundred strains of V. cholerae non-O1/non-O139 serogroups were studied in reaction of slide-agglutination with array of 80 diagnostic sera for non-O1/non-O139 serogroups. Selective screening of strains representing dominating serogroups was performed for extended number of genetic determinants of pathogenicity factors. RESULTS: It was established that V. cholerae belonging to serogroups O53, O67, O75, and O76 are dominating in water ecosystems of Rostov-on-Don city at this time. All studied strains were characterized by lack of cholera toxin genes and toxin-coregulated pili but had different combinations of genes of additional virulence factors. There was no correlation between genotypic characteristics and serogroup. CONCLUSION: The study showed that change of serologic landscape of V. cholerae non-O1/non-O139 occurred in water objects in studied area during last decades. Necessity of dynamic surveillance for circulation of V. cholerae non-O1/non-O139 in aquatic environment with widening of studied spectrum of their biological features was demonstrated.


Subject(s)
Cholera/virology , Environmental Monitoring , Vibrio cholerae non-O1/classification , Vibrio cholerae/classification , Water Microbiology , Cholera/epidemiology , Cholera Toxin/genetics , Epidemiological Monitoring , Fimbriae, Bacterial/genetics , Genes, Bacterial , Humans , Russia/epidemiology , Serotyping , Vibrio cholerae/genetics , Vibrio cholerae/isolation & purification , Vibrio cholerae O139/classification , Vibrio cholerae O139/genetics , Vibrio cholerae O139/isolation & purification , Vibrio cholerae non-O1/genetics , Vibrio cholerae non-O1/isolation & purification , Virulence Factors/genetics
3.
Bioorg Khim ; 17(5): 690-6, 1991 May.
Article in Russian | MEDLINE | ID: mdl-1662954

ABSTRACT

Inhibitors of the angiotensin-converting enzyme were synthesized by substituting N-and C-terminal amino acid residues of tripeptide Bz-Phe-Ala-Pro by the residues of 8-methoxy-5-sulphoquinoline and carboxy-1,2,3,4-tetrahydroquinoline, respectively, and their in vivo and in vitro biological activity was determined. The enzyme's S2' site proved to be non specific to the position of the carboxylic group in the C-terminal heterocyclic part of the inhibitor molecule. Introducing a modified quinoline residue into the N-terminal part of the inhibitor does not increase its specific interaction with the hydrophobic pocket of the angiotensin-converting enzyme.


Subject(s)
Angiotensin-Converting Enzyme Inhibitors/chemical synthesis , Quinolines/chemistry , Angiotensin-Converting Enzyme Inhibitors/metabolism , Angiotensin-Converting Enzyme Inhibitors/pharmacology , Animals , Binding Sites , Captopril/pharmacology , Enalapril/pharmacology , Peptidyl-Dipeptidase A/metabolism , Rats
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