Tendency for oxidation of annelid hemoglobin at alkaline pH and dissociated states probed by redox titration

dc.creatorBispo, JAC
dc.creatorLandini, GF
dc.creatorSantos, JLR
dc.creatorNorberto, DR
dc.creatorBonafe, CFS
dc.date2005
dc.dateAUG
dc.date2014-11-19T22:07:51Z
dc.date2015-11-26T18:06:42Z
dc.date2014-11-19T22:07:51Z
dc.date2015-11-26T18:06:42Z
dc.date.accessioned2018-03-29T00:48:52Z
dc.date.available2018-03-29T00:48:52Z
dc.identifierComparative Biochemistry And Physiology B-biochemistry & Molecular Biology. Elsevier Science Inc, v. 141, n. 4, n. 498, n. 504, 2005.
dc.identifier1096-4959
dc.identifierWOS:000230985900013
dc.identifier10.1016/j.cdpc.2005.06.002
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/78549
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/78549
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/78549
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1293420
dc.descriptionThe redox titration of extracellular hemoglobin of Glossoscolex paulistus (Annelidea) was investigated in different pH conditions and after dissociation induced by pressure. Oxidation increased with increasing PH, as shown by the reduced amount of ferricyanide necessary for the oxidation of hemoglobin. This behavior was the opposite of that of vertebrate hemoglobins. The potential of half oxidation (E 1/2) changed from - 65.3 to + 146.8 mV when the pH increased from 4.50 to 8.75. The functional properties indicated a reduction in the log P-50 from 1.28 to 0.28 in this pH range. The dissociation at alkaline pH or induced by high pressure, confirmed by HPLC gel filtration, suggested that disassembly of the hemoglobin could be involved in the increased potential for oxidation. These results suggest that the high stability and prolonged lifetime common to invertebrate hemoglobins is related to their low tendency to oxidize at acidic pH, in contrast to vertebrate hemoglobins. (c) 2005 Elsevier Inc. All rights reserved.
dc.description141
dc.description4
dc.description498
dc.description504
dc.languageen
dc.publisherElsevier Science Inc
dc.publisherNew York
dc.publisherEUA
dc.relationComparative Biochemistry And Physiology B-biochemistry & Molecular Biology
dc.relationComp. Biochem. Physiol. B-Biochem. Mol. Biol.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectannelid hemoglobin
dc.subjectextracellular hemoglobin
dc.subjecterythrocruorin
dc.subjectdissociated hemoglobin
dc.subjectGlossoscolex paulistus
dc.subjecthemoglobin oxidation
dc.subjectpressure-induced dissociation
dc.subjectredox potential titration
dc.subjectLumbricus-terrestris Hemoglobin
dc.subjectArenicola-marina Polychaeta
dc.subjectExtracellular Hemoglobin
dc.subjectReduction Potentials
dc.subjectEisenia-foetida
dc.subjectHeme Proteins
dc.subjectHydrostatic-pressure
dc.subjectSubunit Structure
dc.subjectOxygen-binding
dc.subjectEarthworm Erythrocruorin
dc.titleTendency for oxidation of annelid hemoglobin at alkaline pH and dissociated states probed by redox titration
dc.typeArtículos de revistas


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