Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/28153
Title: Conformational changes of Loxosceles venom sphingomyelinases monitored by circular dichroism
Authors: Andrade, S. A. de
Pedrosa, MFF
Andrade, RMG de
Oliva, MLV
van den Berge, C. W.
Tambourgi, D. V.
Inst Butantan
Universidade Federal de São Paulo (UNIFESP)
Cardiff Univ
Keywords: Loxosceles
venoms
circular dichroism
sphingomyelinase D
hemolysis
dermonecrosis
Issue Date: 4-Feb-2005
Publisher: Elsevier B.V.
Citation: Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 327, n. 1, p. 117-123, 2005.
Abstract: Envenomation 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.
URI: http://repositorio.unifesp.br/handle/11600/28153
ISSN: 0006-291X
Other Identifiers: http://dx.doi.org/10.1016/j.bbrc.2004.11.146
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