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dc.contributor.authorGarcia, L. T.
dc.contributor.authorSilva, LTPE
dc.contributor.authorRamos, OHP
dc.contributor.authorCarmona, A. K.
dc.contributor.authorBersanetti, P. A.
dc.contributor.authorSelistre-de-Araujo, H. S.
dc.identifier.citationComparative Biochemistry and Physiology C-toxicology & Pharmacology. New York: Elsevier B.V., v. 138, n. 1, p. 23-32, 2004.
dc.description.abstractMetalloproteinases (MPs) are Zn+-dependent endoproteolytic enzymes, abundant in crotalid and viperid snake venoms. Most snake venom metalloproteinases (svMPs) are active on extracellular matrix components and this effect is thought to result in bleeding as a consequence of the basement membrane disruption in capillaries. Jararhagin and ACLH are hemorrhagic svMPs from Bothrops jararaca and Agkistrodon contortrix laticinctus venom, respectively. Both enzymes demonstrate proteolytic activity on fibrinogen and fibronectin and jararhagin inhibits collagen-induced platelet aggregation in vitro. This work describes the expression, purification and successful refolding of the recombinant ACLH zymogen (rPRO-ACLH) as well as the catalytic domain of jararhagin (rCDJARA). the heterologous proteins were produced in E. coli, an in vivo expression system that does not make post-translational modifications. the recombinant refolded proteins did not show any hemorrhagic activity in mice skin, as well as the native deglycosylated jararhagin and ACLH. However, they preserved their proteolytic activity on fibrinogen and fibronectin. It seems that the hemorrhagic properties of these hemorrhagins are dependent on post-translational modifications, whereas their proteolytic activity is not dependent on such modifications. (C) 2004 Elsevier Inc. All rights reserved.en
dc.publisherElsevier B.V.
dc.relation.ispartofComparative Biochemistry and Physiology C-toxicology & Pharmacology
dc.rightsAcesso restrito
dc.subjectsnake venomen
dc.subjectpost-translational modificationen
dc.titleThe effect of post-translational modifications on the hemorrhagic activity of snake venom metalloproteinasesen
dc.contributor.institutionUniversidade Federal de São Carlos (UFSCar)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.description.affiliationUniv Fed Sao Carlos, Dept Ciencias Fisiol, BR-13565905 Sao Carlos, SP, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biofis, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biofis, São Paulo, Brazil
dc.description.sourceWeb of Science

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