info:eu-repo/semantics/article
Hb S-São Paulo: A new sickling hemoglobin with stable polymers and decreased oxygen affinity
Fecha
2012-03Registro en:
Jorge, Susan E. D. C.; Petruk, Ariel Alcides; Kimura, Elza M.; Oliveira, Denise M.; Caire, Lucas; et al.; Hb S-São Paulo: A new sickling hemoglobin with stable polymers and decreased oxygen affinity; Elsevier Science Inc; Archives of Biochemistry and Biophysics; 519; 1; 3-2012; 23-31
0003-9861
CONICET Digital
CONICET
Autor
Jorge, Susan E. D. C.
Petruk, Ariel Alcides
Kimura, Elza M.
Oliveira, Denise M.
Caire, Lucas
Suemasu, Cintia N.
Silveira, Paulo A. A.
Albuquerque, Dulcineia M.
Costa, Fernando F.
Skaf, Munir S.
Martínez, Leandro
De Fatima Sonati, Maria
Resumen
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