Characterization of a hemagglutinating glycoprotein isolated from Bothrops moojeni snake venom

dc.creatorKassab, BH
dc.creatorde Carvalho, DD
dc.creatorMarangoni, S
dc.creatorNovello, JC
dc.date2001
dc.dateFEB
dc.date2014-12-02T16:27:26Z
dc.date2015-11-26T18:01:17Z
dc.date2014-12-02T16:27:26Z
dc.date2015-11-26T18:01:17Z
dc.date.accessioned2018-03-29T00:42:49Z
dc.date.available2018-03-29T00:42:49Z
dc.identifierProtein And Peptide Letters. Bentham Science Publ Ltd, v. 8, n. 1, n. 13, n. 20, 2001.
dc.identifier0929-8665
dc.identifierWOS:000166906400002
dc.identifier10.2174/0929866013409760
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/62797
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/62797
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/62797
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1291942
dc.descriptionFrom the crude snake venom of Bothrops moojeni, a homodimeric lectin was purified by affinity chromatography in lactose and was named BMooL. This lectin appeared to be a glycoprotein because it reacted with Schiffs reagent. The hemagglutinating activity of BMooL is inhibited by galactoside, EDTA, EGTA and DTT. The amino acid analysis of BMooL showed a high content of acidic residues and its N-terminal sequence showed similarity with other lectins from snake venoms.
dc.description8
dc.description1
dc.description13
dc.description20
dc.languageen
dc.publisherBentham Science Publ Ltd
dc.publisherHilversum
dc.publisherHolanda
dc.relationProtein And Peptide Letters
dc.relationProtein Pept. Lett.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectBinding Lectin
dc.subjectJararacussu
dc.subjectBotrocetin
dc.titleCharacterization of a hemagglutinating glycoprotein isolated from Bothrops moojeni snake venom
dc.typeArtículos de revistas


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