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dc.contributor.authorAndrade, S. A. de
dc.contributor.authorPedrosa, MFF
dc.contributor.authorAndrade, RMG de
dc.contributor.authorOliva, MLV
dc.contributor.authorvan den Berge, C. W.
dc.contributor.authorTambourgi, D. V.
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 327, n. 1, p. 117-123, 2005.
dc.description.abstractEnvenomation by arachnids of the genus Loxosceles can induce a variety of biological effects, including dermonecrosis and hemolysis. We have previously identified in L. intermedia venom two highly homologous proteins with sphingomyelinase activity, termed P1 and P2, responsible for all these pathological events, and also an inactive isoform P3. the toxins P1 and P2 displayed 85% identity with each other at the amino acid level and showed a 57% identity with SMase I, an active toxin from L. laeta venom. Circular dichroism was used to determine and compare the solution structure of the active and inactive isoforms. Effects of pH and temperature change on the CD spectra of the toxins were investigated and correlated with the biological activities. This study sheds new light on the structure-function relationship of homologous proteins with distinct biological properties and represents the first report on the structure-function relationship of Loxosceles sphingomyelinases D. (C) 2004 Elsevier Inc. All rights reserved.en
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.rightsAcesso restrito
dc.subjectcircular dichroismen
dc.subjectsphingomyelinase Den
dc.titleConformational changes of Loxosceles venom sphingomyelinases monitored by circular dichroismen
dc.contributor.institutionInst Butantan
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionCardiff Univ
dc.description.affiliationInst Butantan, Lab Imunoquim, São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Lab Bioquim, São Paulo, Brazil
dc.description.affiliationCardiff Univ, Wales Coll Med, Dept Pharmacol Toxicol & Therapeut, Cardiff, S Glam, Wales
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Lab Bioquim, São Paulo, Brazil
dc.description.sourceWeb of Science
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