Conformational changes of Loxosceles venom sphingomyelinases monitored by circular dichroism
Biochem. biophys. res. commun
; 327(1): 117-123, 2005.
Article
in English
| Sec. Est. Saúde SP, SESSP-IBPROD, Sec. Est. Saúde SP, SESSP-IBACERVO
| ID: biblio-1060799
Responsible library:
BR78.1
Localization: BR78.1
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 structurefunction relationship of homologous proteins with distinct biological properties and represents the first report on the structurefunction relationship of Loxosceles sphingomyelinases D.
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Collection:
National databases
/
Brazil
Database:
Sec. Est. Saúde SP
/
SESSP-IBACERVO
/
SESSP-IBPROD
Main subject:
Poisons
/
Spiders
Limits:
Animals
Language:
English
Journal:
Biochem. biophys. res. commun
Year:
2005
Document type:
Article
Institution/Affiliation country:
Instituto Butantan/BR