Rattlesnake hemoglobins: Functional properties and tetrameric stability

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade Estadual de Campinas (UNICAMP)
dc.contributorCtr Univ jales
dc.date.accessioned2014-05-20T14:03:01Z
dc.date.available2014-05-20T14:03:01Z
dc.date.created2014-05-20T14:03:01Z
dc.date.issued2006-01-01
dc.identifierProtein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 13, n. 5, p. 517-523, 2006.
dc.identifier0929-8665
dc.identifierhttp://hdl.handle.net/11449/22207
dc.identifier10.2174/092986606776819484
dc.identifierWOS:000237935900018
dc.identifier2406867656111498
dc.description.abstractThe present work analyzed the tetrameric stability of the hemoglobins from the rattlesnake C. durissus terrificus using analytical gel filtration chromatography, SAXS and osmotic stress. We show that the dissociation mechanism proposed for L. miliaris hemoglobin does not apply for these hemoglobins, which constitute stable tetramers even at low concentrations.
dc.languageeng
dc.publisherBentham Science Publ Ltd
dc.relationProtein and Peptide Letters
dc.relation1.039
dc.relation0,429
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjecthemoglobin
dc.subjectrattlesnake
dc.subjecttetramer stability
dc.titleRattlesnake hemoglobins: Functional properties and tetrameric stability
dc.typeArtículos de revistas


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