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ISOLATION OF AN OPHIDIAN PARAMYXOVIRUS (OPMV) IN A CAPTIVE RATTLESNAKE (Crotalus durissus terrificus) FROM BOTUCATU, SÃO PAULO STATE, BRAZIL J. Venom. Anim. Toxins
NOGUEIRA,M. F.; BARRELLA,T. H.; SILVA,R. J. DA; LOPES,C. A. M.; ARAÚJO JÚNIOR,J. P..
This study reports the isolation of an Ophidian Paramyxovirus (OPMV) in sputum of a captive rattlesnake (Crotalus durissus terrificus) kept in a serpentarium located in Botucatu, São Paulo State, Brazil. Polymerase chain reaction (PCR) and nested-PCR were performed for the identification of the isolated virus.
Tipo: Info:eu-repo/semantics/other Palavras-chave: Crotalus durissus terrificus; Rattlesnake; Paramyxovirus; Ophidian Paramyxovirus; Hemagglutination; Polymerase chain reaction.
Ano: 2002 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0104-79302002000100013
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Isolation and Characterization of Midgut Lectin From Aedes aegypti (L.) (Diptera: Culicidae) BABT
Ayaad,Tahany Hassan; Al-Akeel,Rasha Khalifah; Olayan,Ebtisam.
ABSTRACT The present investigation deals with the isolation and characterization of a lectin from Aedes aegypti (Ae aegypti) female mid gut extract that agglutinates various mammalian red blood cells (RBCs) such as human three groups A, B, and O (RH+), mouse, rat, guinea-pig, sheep and goat erythrocytes. The highest activity of both crude and isolated mid gut lectins were detected against sheep RBCs. Using (NH4)2 SO4 fractionation, ion-exchange and mannose-CNBr-Sepharose 6B affinity chromatography techniques, Ae. aegypti midgut lectin (Aelec) was purified to homogeneity.Isoelectric focusing (IEF) and reducing SDS/PAGE revealed that the isolated mid gut lectin had isoelectric point (PI) of 5.90, and subunits approximate molecular weights of 35.50 and 27.35...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Lectin; Purification; Characterization; Hemagglutination; Aedes aegypti; Mosquitoes.
Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000600905
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Lectin activity in mycelial extracts of Fusarium species BJM
Bhari,Ranjeeta; Kaur,Bhawanpreet; Singh,Ram S..
ABSTRACT Lectins are non-immunogenic carbohydrate-recognizing proteins that bind to glycoproteins, glycolipids, or polysaccharides with high affinity and exhibit remarkable ability to agglutinate erythrocytes and other cells. In the present study, ten Fusarium species previously not explored for lectins were screened for the presence of lectin activity. Mycelial extracts of F. fujikuroi, F. beomiformii, F. begoniae, F. nisikadoi, F. anthophilum, F. incarnatum, and F. tabacinum manifested agglutination of rabbit erythrocytes. Neuraminidase treatment of rabbit erythrocytes increased lectin titers of F. nisikadoi and F. tabacinum extracts, whereas the protease treatment resulted in a significant decline in agglutination by most of the lectins. Results of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Fusarium; Lectin; Hemagglutination; Carbohydrate specificity; Culture age.
Ano: 2016 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822016000300775
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