dc.creatorTorsoni, M A
dc.creatorSouza-Torsoni, A
dc.creatorOgo, S H
dc.date1998-Apr
dc.date2015-11-27T12:19:12Z
dc.date2015-11-27T12:19:12Z
dc.date.accessioned2018-03-29T00:52:44Z
dc.date.available2018-03-29T00:52:44Z
dc.identifierBiochemistry And Molecular Biology International. v. 44, n. 4, p. 851-60, 1998-Apr.
dc.identifier1039-9712
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/9584999
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194160
dc.identifier9584999
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294393
dc.descriptionGeochelone carbonaria hemoglobin (Hb) was analyzed by polyacrylamide gel electrophoresis (PAGE) and purified by ion exchange chromatography on CM-cellulose. Seven fractions were obtained using fresh Hb preparations. CM-cellulose chromatography of Hb reacted with iodoacetamide, showed one minor (HbI) and one major band (HbII). Analysis of the molecular masses of recently collected Hb and of aged solutions determined by gel filtration showed that polymerization increased with the duration of storage. The reaction with oxidized glutathione changed the electrophoretic pattern of Hb, and highlighted the bands corresponding to glutathionyl-Hb. The presence of these bands in fresh Hb solutions and in alkylated preparations suggests that they may occur in vivo. PAGE under dissociating conditions showed that the hemolysate contained 3 different polypeptide chains (G1, G2 and G3). Both Hb components shared the G1 globin chain with HbI containing G1 and G2 and HbII, G1 and G3 chains.
dc.description44
dc.description851-60
dc.languageeng
dc.relationBiochemistry And Molecular Biology International
dc.relationBiochem. Mol. Biol. Int.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAnimals
dc.subjectDisulfides
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectErythrocytes
dc.subjectGlutathione Disulfide
dc.subjectHemoglobins
dc.subjectOxidation-reduction
dc.subjectSulfhydryl Compounds
dc.subjectTurtles
dc.titleInvolvement Of Available Sh Groups In The Heterogeneity Of Hemoglobin From The Tortoise Geochelone Carbonaria.
dc.typeArtículos de revistas


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