Urea-induced unfolding of Glossoscolex paulistus hemoglobin, in oxy- and cyanomet-forms: A dissociation model

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorCarvalho, Francisco A.O.
dc.creatorCarvalho, José Wilson P.
dc.creatorSantiago, Patrícia S.
dc.creatorTabak, Marcel
dc.date2014-05-27T11:27:28Z
dc.date2016-10-25T18:40:56Z
dc.date2014-05-27T11:27:28Z
dc.date2016-10-25T18:40:56Z
dc.date2013-01-01
dc.date.accessioned2017-04-06T02:07:09Z
dc.date.available2017-04-06T02:07:09Z
dc.identifierInternational Journal of Biological Macromolecules, v. 52, n. 1, p. 340-348, 2013.
dc.identifier0141-8130
dc.identifier1879-0003
dc.identifierhttp://hdl.handle.net/11449/74173
dc.identifierhttp://acervodigital.unesp.br/handle/11449/74173
dc.identifier10.1016/j.ijbiomac.2012.09.023
dc.identifierWOS:000313934300050
dc.identifier2-s2.0-84869410588.pdf
dc.identifier2-s2.0-84869410588
dc.identifierhttp://dx.doi.org/10.1016/j.ijbiomac.2012.09.023
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/894946
dc.descriptionThe urea effect on the giant extracellular hemoglobin of Glossoscolex paulistus (HbGp) stability was studied by analytical ultracentrifugation (AUC) and small angle X-ray scattering (SAXS). AUC data show that the sedimentation coefficient distributions curves c (S), at 1.0mol/L of urea, display a single peak at 57 S, associated to the undissociated protein. The increase in urea concentration, up to 4.0mol/L, induces the appearance of smaller species, due to oligomeric dissociation. The sedimentation coefficients and molecular masses are 9.2S and 204kDa for the dodecamer (abcd)3, 5.5S and 69kDa for the tetramer (abcd), 4.1S and 52kDa for the trimer (abc) and 2.0 S and 17kDa for the monomer d, respectively. SAXS data show initially a decrease in the I(0) values due to the oligomeric dissociation, and then, above 4.0mol/L of denaturant, for oxy-HbGp, and above 6.0mol/L for cyanomet-HbGp, an increase in the maximum dimension and gyration radius is observed, due to the unfolding process. According to AUC and SAXS data the HbGp unfolding is described by two phases: the first one, at low urea concentration, below 4.0mol/L, characterizes the oligomeric dissociation, while the second one, at higher urea concentration, is associated to the unfolding of dissociated species. Our results are complementary to a recent report based on spectroscopic observations. © 2012 Elsevier B.V.
dc.languageeng
dc.relationInternational Journal of Biological Macromolecules
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectAUC
dc.subjectExtracellular hemoglobin
dc.subjectHbGp
dc.subjectOligomeric dissociation
dc.subjectSAXS
dc.subjectUrea
dc.subjectcyanomethemoglobin
dc.subjecthemoglobin
dc.subjectoxyhemoglobin
dc.subjectunclassified drug
dc.subjecturea
dc.subjectannelid
dc.subjectconcentration response
dc.subjectdissociation
dc.subjectGlossoscolex paulistus
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectoligomeric dissociation
dc.subjectprotein stability
dc.subjectprotein structure
dc.subjectprotein unfolding
dc.subjectsedimentation
dc.subjectultracentrifugation
dc.subjectX ray crystallography
dc.subjectAnimals
dc.subjectHemoglobins
dc.subjectModels, Chemical
dc.subjectOligochaeta
dc.subjectProtein Folding
dc.subjectGlossoscolex
dc.titleUrea-induced unfolding of Glossoscolex paulistus hemoglobin, in oxy- and cyanomet-forms: A dissociation model
dc.typeOtro


Este ítem pertenece a la siguiente institución