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| Oliveira,T.M.; Souza,F.P.; Jardim,A.C.G.; Cordeiro,J.A.; Pinho,J.R.R.; Sitnik,R.; Estevão,I.F.; Bonini-Domingos,C.R.; Rahal,P.. |
| Hereditary hemochromatosis is a disorder of iron metabolism characterized by increased iron intake and progressive storage and is related to mutations in the HFE gene. Interactions between thalassemia and hemochromatosis may further increase iron overload. The ethnic background of the Brazilian population is heterogeneous and studies analyzing the simultaneous presence of HFE and thalassemia-related mutations have not been carried out. The aim of this study was to evaluate the prevalence of the H63D, S65C and C282Y mutations in the HFE gene among 102 individuals with alpha-thalassemia and 168 beta-thalassemia heterozygotes and to compare them with 173 control individuals without hemoglobinopathies. The allelic frequencies found in these three groups were... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: HFE; H63D; S65C; C282Y; Thalassemia. |
| Ano: 2006 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2006001200008 |
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| Tosqui,P.; Bonini-Domingos,C.R.; Colombo,M.F.. |
| The role of chloride in the stabilization of the deoxy conformation of hemoglobin (Hb), the low oxygen affinity state, has been studied in order to identify the nature of this binding. Previous studies have shown that arginines 141α could be involved in the binding of this ion to the protein. Thus, des-Arg Hb, human hemoglobin modified by removal of the α-chain C-terminal residue Arg141α, is a possible model for studies of these interactions. The loss of Arg141α and all the salt bridges in which it participates is associated with subtle structural perturbations of the α-chains, which include an increase in the conformational flexibility and further shift to the oxy state, increasing oxygen affinity. Thus, this Hb has been the target of many studies of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Des-Arg hemoglobin; Oxygen affinity. |
| Ano: 2009 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2009000600004 |
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