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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/21961
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dc.contributor.authorBortoleto, R. K.-
dc.contributor.authorMurakami, M. T.-
dc.contributor.authorWatanabe, L.-
dc.contributor.authorSoares, A. M.-
dc.contributor.authorArni, R. K.-
dc.date.accessioned2014-05-20T14:02:19Z-
dc.date.accessioned2016-10-25T17:09:01Z-
dc.date.available2014-05-20T14:02:19Z-
dc.date.available2016-10-25T17:09:01Z-
dc.date.issued2002-09-01-
dc.identifierhttp://dx.doi.org/10.1016/S0041-0101(02)00140-X-
dc.identifier.citationToxicon. Oxford: Pergamon-Elsevier B.V., v. 40, n. 9, p. 1307-1312, 2002.-
dc.identifier.issn0041-0101-
dc.identifier.urihttp://hdl.handle.net/11449/21961-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/21961-
dc.description.abstractA fibrinogen-clotting enzyme, Jararacussin-I, was purified from the venom of Bothrops jararacussu by a combination of ion exchange chromatography using Resource 15S resin and affinity chromatography using Benzamidine Sepharose 6B resin. Jararacussin-I displays a molecular mass of 28 kDa as estimated by sodium dodecyl sulphate-PAGE and possesses an isoetectric point of 5.0. The coagulant specific activity of the enzyme was determined to be 45.8 NIH U/mg using bovine fibrinogen as the substrate and the esterase specific activity was determined to be 258.7 U/mg. The protease inhibitors, benzamidine and DTT inhibited the esterase specific activity by 72.4 and 69.7%, respectively. The optimal temperature and pH for the degradation of both chains of fibrinogen and esterase specific activity were determined to be 37 degreesC and 7.4-8.0, respectively. The enzyme was inactivated at both 4 and 75 T. Single crystals of Jararacussin-I were obtained and complete three-dimensional X-ray diffraction data was collected at the Brazilian National Synchrotron Source (LNLS) to a resolution of 2.4 Angstrom. (C) 2002 Published by Elsevier B.V. Ltd.en
dc.format.extent1307-1312-
dc.language.isoeng-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectBothrops jararacussu snake venompt
dc.subjectthrombin-like enzymept
dc.subjectfibrinogen-clotting enzymept
dc.subjectpurificationpt
dc.subjectcharacterization and crystallizationpt
dc.titlePurification, characterization and crystallization of Jararacussin-I, a fibrinogen-clotting enzyme isolated from the venom of Bothrops jararacussuen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUNAERP-
dc.description.affiliationUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUNAERP, Dept Biotechnol, Ribeirao Preto, Brazil-
dc.description.affiliationUnespUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.identifier.doi10.1016/S0041-0101(02)00140-X-
dc.identifier.wosWOS:000178603500008-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofToxicon-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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