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dc.contributor.authorGouveia, AID
dc.contributor.authorSilveira, R. B. da
dc.contributor.authorNader, H. B.
dc.contributor.authorDietrich, C. P.
dc.contributor.authorGremski, W.
dc.contributor.authorVeiga, S. S.
dc.identifier.citationToxicon. Oxford: Pergamon-Elsevier B.V., v. 45, n. 4, p. 403-410, 2005.
dc.description.abstractBy studying Lonomia obliqua (caterpillar) venom we were able to detect a lytic activity on purified hyaluronic acid. the venom hydrolyses purified chondroitin sulphate, but was unable to degrade either heparan sulphate or dermatan sulphate. Moreover, through purified hyaluronic acid-degrading kinetic assays, we observed that this lytic activity was caused by a hydrolase rather than lyase enzyme. in addition, by using the Reissig colorimetric reaction, we detected this hyaluronic acid hydrolase action as a beta-endohexosaminidase enzyme originating terminal N-acetylglucosamine residues rather than beta-endoglucuronidase, which may originate glucuronic acid residues. Zymogram analysis of the venom detected 49 and 53 kDa molecules with hyaluronic acid lyric activity. An examination of these hyaluronic acid degrading activities as a function of pH showed that these hydrolases had no apparent activities at a pH below 5.0 and higher than 8.0 and displayed their optimal activities at pH ranging from 6.0 to 7.0. Finally, through a fluorescence reaction to hyaluronic acid and confocal microscopy, we confirmed this cleaving action upon hyaluronic acid organised on the extracellular matrix of the dermis of rabbit. the data provide experimental evidence of the presence of hyaluronidases in the L. obliqua venom, probably involved in the harmful effects of the venom. (c) 2004 Published by Elsevier B.V.en
dc.publisherElsevier B.V.
dc.rightsAcesso restrito
dc.subjectLonomia obliquaen
dc.titleIdentification and partial characterisation of hyaluronidases in Lonomia obliqua venomen
dc.contributor.institutionUniv Fed Parana
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionCatholic Univ Parana
dc.description.affiliationUniv Fed Parana, Dept Cell Biol, BR-81531990 Curitiba, Parana, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biochem, São Paulo, Brazil
dc.description.affiliationCatholic Univ Parana, Hlth & Biol Sci Inst, Curitiba, Parana, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biochem, São Paulo, Brazil
dc.description.sourceWeb of Science

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