Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/90092
Type: Artigo de periódico
Title: Hb S-são Paulo: A New Sickling Hemoglobin With Stable Polymers And Decreased Oxygen Affinity
Author: Jorge S.E.D.C.
Petruk A.A.
Kimura E.M.
Oliveira D.M.
Caire L.
Suemasu C.N.
Silveira P.A.A.
Albuquerque D.M.
Costa F.F.
Skaf M.S.
Martinez L.
De Fatima Sonati M.
Abstract: Hb S-São Paulo (SP) [HBB:c.20A > T p.Glu6Val; c.196A > G p.Lys65Glu] is a new double-mutant hemoglobin that was found in heterozygosis in an 18-month-old Brazilian male with moderate anemia. It behaves like Hb S in acid electrophoresis, isoelectric focusing and solubility testing but shows different behavior in alkaline electrophoresis, cation-exchange HPLC and RP-HPLC. The variant is slightly unstable, showed reduced oxygen affinity and also appeared to form polymers more stable than the Hb S. Molecular dynamics simulation suggests that the polymerization is favored by interfacial electrostatic interactions. This provides a plausible explanation for some of the reported experimental observations. © 2012 Elsevier Inc. All rights reserved.
Editor: 
Rights: fechado
Identifier DOI: 10.1016/j.abb.2012.01.001
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-84857277089&partnerID=40&md5=bad01a848be1aaae8b0635cfb70cd8fc
Date Issue: 2012
Appears in Collections:Unicamp - Artigos e Outros Documentos

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