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Cholesterol-dependent hemolytic activity of Passiflora quadrangularis leaves BJMBR
Yuldasheva,L.N.; Carvalho,E.B.; Catanho,M.-T.J.A.; Krasilnikov,O.V..
Plants used in traditional medicine are rich sources of hemolysins and cytolysins, which are potential bactericidal and anticancer drugs. The present study demonstrates for the first time the presence of a hemolysin in the leaves of Passiflora quadrangularis L. This hemolysin is heat stable, resistant to trypsin treatment, has the capacity to froth, and acts very rapidly. The hemolysin activity is dose-dependent, with a slope greater than 1 in a double-logarithmic plot. Polyethylene glycols of high molecular weight were able to reduce the rate of hemolysis, while liposomes containing cholesterol completely inhibited it. In contrast, liposomes containing phosphatidylcholine were ineffective. The Passiflora hemolysin markedly increased the conductance of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Passiflora quadrangularis; Leaf extract; Liposomes; Bilayer permeation; Hemolysin; Membrane cholesterol.
Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000700009
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Skin secretion of Siphonops paulensis (Gymnophiona, Amphibia) forms voltage-dependent ionic channels in lipid membranes BJMBR
Schwartz,E.F.; Stucchi-Zucchi,A.; Schwartz,C.A.; Salomão,L.C..
The effect of the skin secretion of the amphibian Siphonops paulensis was investigated by monitoring the changes in conductance of an artificial planar lipid bilayer. Skin secretion was obtained by exposure of the animals to ether-saturated air, and then rinsing the animals with distilled water. Artificial lipid bilayers were obtained by spreading a solution of azolectin over an aperture of a Delrin cup inserted into a cut-away polyvinyl chloride block. In 9 of 12 experiments, the addition of the skin secretion to lipid bilayers displayed voltage-dependent channels with average unitary conductance of 258 ± 41.67 pS, rather than nonspecific changes in bilayer conductance. These channels were not sensitive to...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Siphonops; Toxin; Channel-forming toxins; Skin secretion; Ion channel; Hemolysin.
Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2003000900020
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Role of wild birds as carriers of multi-drug resistant Escherichia coli and Escherichia vulneris BJM
Shobrak,Mohammed Y.; Abo-Amer,Aly E..
Emergence and distribution of multi-drug resistant (MDR) bacteria in environments pose a risk to human and animal health. A total of 82 isolates of Escherichia spp. were recovered from cloacal swabs of migrating and non-migrating wild birds. All bacterial isolates were identified and characterized morphologically and biochemically. 72% and 50% of isolates recovered from non-migrating and migrating birds, respectively, showed positive congo red dye binding (a virulence factor). Also, hemolysin production (a virulence factor) was showed in 8% of isolates recovered from non-migrating birds and 75% of isolates recovered from migrating birds. All isolates recovered from non-migrating birds were found resistant to Oxacillin while all isolates recovered from...
Tipo: Info:eu-repo/semantics/article Palavras-chave: E. coli; E. vulneris; Multi-drug resistance (MDR); Migrating and non-migrating birds; Congo red binding; Hemolysin; API 20E; 16S rRNA; Plasmid profile.
Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822014000400010
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Virulence-associated characteristics of Enterococcus faecalis strains isolated from clinical sources BJM
Furumura,Márcia T.; Figueiredo,Patricia M.S.; Carbonell,Gleize V.; Darini,Ana Lucia da Costa; Yano,Tomomasa.
Thirty-two clinical isolates of Enterococcus faecalis were screened for virulence factors. Twenty-four (75%) isolates produced hemolysin on Mueller-Hinton blood agar plates with sheep erythrocytes. However, the cell free heat-stable hemolysin was detected in all isolates (100%) of E. faecalis when grown in BHI-GA (BHI medium supplemented with 1% glucose and 0.03% L-arginine), but not in BHI broth alone. Twenty-four isolates (75%) produced caseinase and 23 (71.9%) lipase, but none of the isolates produced gelatinase. Fifteen (46.9%) culture filtrates caused rounding and membrane alterations with blebbing formation followed by death in HeLa and HEp-2 cells, but not in Vero cells. Thirteen isolates (40.6%) agglutinated rabbit erythrocytes, but did not produce...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Enterococcus faecalis; Virulence factors; Hemolysin; Proteases; Lipase; Cytotoxin; Biofilm.
Ano: 2006 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822006000300007
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Amplification of tlh gene in other Vibrionaceae specie by specie-specific multiplex PCR of Vibrio parahaemolyticus Electron. J. Biotechnol.
Yáñez,Romina; Bastías,Roberto; Higuera,Gastón; Salgado,Oscar; Katharios,Pantelis; Romero,Jaime; Espejo,Romilio; García,Katherine.
Background The surveillance of Vibrio parahaemolyticus in the Chilean coast has been mainly performed by multiplex PCR amplification of three different hemolysin genes, which are specie-specific virulence factors. These genes are also employed in the determination of V. parahaemolyticus pathogenic load in seafood and for characterization of pathogenic strains associated to diarrhea cases in human. During environmental surveillance that we performed every summer, we occasionally observed a thermolabile hemolysin (tlh) PCR product of a slightly smaller size than expected, which was coincident with low loads of V. parahaemolyticus in the environment. In order to understand this observation, we probed the specificity of tlh primers for the detection of V....
Tipo: Journal article Palavras-chave: Hemolysin; Multiplex PCR; Pathogen surveillance; Virulence factor; Vibrio parahaemolyticus.
Ano: 2015 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582015000600012
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Characterization, purification and phylogenetic analysis of a cytolysin from the sea anemone Heteractis magnifica of the Indian Ocean J. Venom. Anim. Toxins incl. Trop. Dis.
Karthikayalu,S; Rama,V; Kirubagaran,R; Venkatesan,R.
It is well established that sea anemones comprise a rich source of cytolytic toxins. The present study reports the isolation and characterization of a cytolysin obtained from the sea anemone Heteractis magnifica collected in the Andaman Islands of the Indian Ocean. The crude extract was screened for hemolytic activity by a blood agar plate method and a 6-mm zone of clearance was observed after incubation. The hemolytic property of the crude extract, tested by the microtiter plate method, revealed positive results at concentrations as low as 120 ng/mL. Furthermore, it was favored by alkaline pH and was stable up to 60°C. On the other hand, the hemolytic effect was abolished by the addition of human serum. Purification steps involved ammonium sulfate...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Heteractis magnifica; Marine toxin; Hemolysin; Cytolysin.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992010000200006
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Purification of a 19-kDa pore-forming cytolysin from the sea anemone Heteractis magnifica J. Venom. Anim. Toxins incl. Trop. Dis.
Karthikayalu,S; Rama,V; Venkatesan,R.
Pore-forming cytolysins of 19 kDa from sea anemones present a remarkable cytolytic property. In the present work, a purified 19-kDa cytolysin was obtained from the sea anemone Heteractis magnifica. The purification steps involved ammonium sulfate precipitation and subsequently desalting by dialysis against 10 mM sodium phosphate buffer (pH 7.4), followed by anion exchange chromatography in DEAE-Sepharose® column (GE Healthcare, Sweden) and gel filtration chromatography using Sephadex® G-50 matrix (GE Healthcare, Sweden). The active fractions from the gel filtration chromatography were pooled and rechromatographed in the same column. The final active fraction showed a prominent protein band of molecular mass of 19 kDa when analyzed by SDS-PAGE.
Tipo: Info:eu-repo/semantics/other Palavras-chave: Heteractis magnifica; Cytolysin; Hemolysin; Pore-forming toxin.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992010000300019
Registros recuperados: 7
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