Functional and structural analysis of two fibrinogen-activating enzymes isolated from the venoms of Crotalus durissus terrificus and Crotalus durissus collilineatus

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorde Oliveira, Daniela G. L.
dc.creatorMurakami, Mario T.
dc.creatorCintra, Adelia C. O.
dc.creatorFranco, Joao J.
dc.creatorSampaio, Suely V.
dc.creatorArni, Raghuvir K.
dc.date2014-05-20T15:32:20Z
dc.date2016-10-25T18:08:32Z
dc.date2014-05-20T15:32:20Z
dc.date2016-10-25T18:08:32Z
dc.date2009-01-01
dc.date.accessioned2017-04-06T00:27:09Z
dc.date.available2017-04-06T00:27:09Z
dc.identifierActa Biochimica Et Biophysica Sinica. Oxford: Oxford Univ Press, v. 41, n. 1, p. 21-29, 2009.
dc.identifier1672-9145
dc.identifierhttp://hdl.handle.net/11449/41267
dc.identifierhttp://acervodigital.unesp.br/handle/11449/41267
dc.identifier10.1093/abbs/gmn003
dc.identifierWOS:000264455000003
dc.identifierhttp://dx.doi.org/10.1093/abbs/gmn003
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/883979
dc.descriptionFibrinogen-activating enzymes, widely distributed in Crotalidae and Viperidae venoms, are single-chain glycosylated serine proteases that display high macromolecular selectivity and are often referred to as thrombin-like enzymes (TLEs). TLEs serve as structural models to extend our understanding of the structure-function relationships of blood coagulation factors, have been clinically used for the treatment of thrombotic diseases, and are used as tools in clinical assays. The combination of gel filtration and ion-exchange chromatography proved to be successful in obtaining milligram quantities of pure samples of TLEs from the venoms of Crotalus durissus terrificus ( white venom) and Crotalus durissus collilineatus ( yellow venom). Functional characterization indicates that both enzymes preferentially degrade the B beta chain of bovine fibrinogen and possess edema-inducing and coagulant activities. However, the TLE from C. d. collilineatus venom shows twofold higher coagulant activity with a minimum coagulant dose (MCD) of 0.6 mg/ml, whereas the enzyme isolated from C. d. terrificus indicated an MCD of 1.5 mg/ml. Molecular modeling of gyroxin and structural comparisons with other highly conserved snake venom serine proteases, underlines the key role played by the surface charge distribution and the double insertion in the 174-surface loop in macromolecular substrate recognition by TLEs.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageeng
dc.publisherOxford University Press
dc.relationActa Biochimica et Biophysica Sinica
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectCrotalus durissus sp
dc.subjectthrombin-like enzyme
dc.subjectfunctional characterization
dc.subjectcrystallization
dc.subjectMolecular modeling
dc.titleFunctional and structural analysis of two fibrinogen-activating enzymes isolated from the venoms of Crotalus durissus terrificus and Crotalus durissus collilineatus
dc.typeOtro


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