A rapid procedure for the isolation of the Lys-49 myotoxin II from Bothrops moojeni (caissaca) venom: Biochemical characterization, crystallization, myotoxic and edematogenic activity

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dc.contributor.authorSoares, A. M.
dc.contributor.authorRodrigues, V. M.
dc.contributor.authorHomsi-Brandeburgo, M. I.
dc.contributor.authorToyama, M. H.
dc.contributor.authorLombardi, F. R.
dc.contributor.authorArni, R. K.
dc.contributor.authorGiglio, JR
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de Uberlândia (UFU)
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T15:24:11Z
dc.date.available2014-05-20T15:24:11Z
dc.date.issued1998-03-01
dc.description.abstractA, M. Soares, V, M, Rodrigues, M. I. Homsi-Brandeburgo, M. H. Toyama, F, R, Lombardi, K. Arni and J. R, Giglio. A rapid procedure for the isolation of the Lys-49 myotoxin II from Bothrops moojeni (caissaca) venom: Biochemical characterization, crystallization, myotoxic and edematogenic activity. Toxicon 36, 503-514, 1998.-Bothrops moojeni snake venom was fractionated on a CM-Sepharose column which was previously equilibrated with 0.05 M ammonium bicarbonate buffer at pH 8.0 and subsequently eluted with an ammonium bicarbonate concentration gradient from 0.05 to 0.5 M at constant pH (8.0) and temperature (25 degrees C). The fraction which eluted last (M-VI) showed, after direct lyophilization, a single band by polyacrylamide gel electrophoresis (PAGE) and SDS-PAGE, indicating an approximate M,. of 14 000 and 77 000, in the presence and absence of dithiothreitol, respectively. Its amino acid composition revealed a high level of hydrophobic and basic amino acids as well as 13 half-cystine residues. Its isoelectric point and extinction coefficient (E-1.0cm(1.0mg/ml) at 278 nm and pH 7.0) were 8.2 and 1.170, respectively. M-VI was devoid of phospholipase A(2) (PLA(2)) activity on egg yolk, as well as of hemorrhagic, anticoagulant and coagulant activities, but could induce drastic necrosis on skeletal muscle fibres as well as rapid and transient edema on the rat paw. Its N-terminal sequence: SLFELGKMILQETGKNPAKSYGVYGCNCGVGGRGKPKDATDRCCYVHKCCYK.... revealed high homology with other Lys 49 PLA(2)-like myotoxins from other bothropic venoms. Orthorhombic crystals of M-VI? which diffracted to a maximal resolution of 1.6 Angstrom. were obtained and indicated the presence of a dimer in the asymmetrical unit. (C) 1998 Elsevier B.V. Ltd. All rights reserved.en
dc.description.affiliationUniv São Paulo, Fac Med, Dept Bioquim, BR-14049900 Ribeirao Preto, SP, Brazil
dc.description.affiliationUniversidade Federal de Uberlândia (UFU), Dept Genet & Bioquim, BR-38400 Uberlandia, MG, Brazil
dc.description.affiliationUniv Campinas, Inst Biol, Dept Bioquim, Campinas, SP, Brazil
dc.description.affiliationUniv Estadual Paulista, IBILCE, Dept Fis, Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, IBILCE, Dept Fis, Sao Jose do Rio Preto, SP, Brazil
dc.format.extent503-514
dc.identifierhttp://dx.doi.org/10.1016/S0041-0101(97)00133-5
dc.identifier.citationToxicon. Oxford: Pergamon-Elsevier B.V., v. 36, n. 3, p. 503-514, 1998.
dc.identifier.doi10.1016/S0041-0101(97)00133-5
dc.identifier.issn0041-0101
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/34829
dc.identifier.wosWOS:000074439600008
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofToxicon
dc.relation.ispartofjcr2.352
dc.relation.ispartofsjr0,692
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.titleA rapid procedure for the isolation of the Lys-49 myotoxin II from Bothrops moojeni (caissaca) venom: Biochemical characterization, crystallization, myotoxic and edematogenic activityen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes9162508978945887[6]
unesp.author.orcid0000-0003-2460-1145[6]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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