Purification, characterization and crystallization of Jararacussin-I, a fibrinogen-clotting enzyme isolated from the venom of Bothrops jararacussu

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorBortoleto, R. K.
dc.creatorMurakami, M. T.
dc.creatorWatanabe, L.
dc.creatorSoares, A. M.
dc.creatorArni, R. K.
dc.date2014-05-20T14:02:19Z
dc.date2016-10-25T17:09:01Z
dc.date2014-05-20T14:02:19Z
dc.date2016-10-25T17:09:01Z
dc.date2002-09-01
dc.date.accessioned2017-04-05T21:27:12Z
dc.date.available2017-04-05T21:27:12Z
dc.identifierToxicon. Oxford: Pergamon-Elsevier B.V., v. 40, n. 9, p. 1307-1312, 2002.
dc.identifier0041-0101
dc.identifierhttp://hdl.handle.net/11449/21961
dc.identifierhttp://acervodigital.unesp.br/handle/11449/21961
dc.identifier10.1016/S0041-0101(02)00140-X
dc.identifierWOS:000178603500008
dc.identifierhttp://dx.doi.org/10.1016/S0041-0101(02)00140-X
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/867439
dc.descriptionA 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.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationToxicon
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectBothrops jararacussu snake venom
dc.subjectthrombin-like enzyme
dc.subjectfibrinogen-clotting enzyme
dc.subjectpurification
dc.subjectcharacterization and crystallization
dc.titlePurification, characterization and crystallization of Jararacussin-I, a fibrinogen-clotting enzyme isolated from the venom of Bothrops jararacussu
dc.typeOtro


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