Artículos de revistas
Hb S-Sao Paulo: A new sickling hemoglobin with stable polymers and decreased oxygen affinity
Fecha
2012Registro en:
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, NEW YORK, v. 519, n. 1, supl. 4, Part 1, pp. 23-31, 36951, 2012
0003-9861
10.1016/j.abb.2012.01.001
Autor
Jorge, Susan E. D. C.
Petruk, Ariel A.
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
Sonati, Maria de Fatima
Institución
Resumen
Hb S-Sao 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. (C) 2012 Elsevier Inc. All rights reserved.