Hemoglobin Rahere, a human hemoglobin variant with amino acid substitution at the 2,3-diphosphoglycerate binding site. Functional consequences of the alteration and effects of bezafibrate on the oxygen bindings.

We encountered an abnormal hemoglobin (Rahere), with a threonine residue replacing the beta 82 (EF6) lysine residue at the binding site of 2,3-diphosphoglycerate, which was responsible for overt erythrocytosis in two individuals of a Japanese family. Hemoglobin Rahere shows a lower oxygen affinity o...

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Bibliografische gegevens
Gepubliceerd in:J Clin Invest
Hoofdauteurs: Sugihara, J, Imamura, T, Nagafuchi, S, Bonaventura, J, Bonaventura, C, Cashon, R
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: American Society for Clinical Investigation 1985
Onderwerpen:
Research Article
Online toegang:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC424016/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3930571/
https://ncbi.nlm.nih.govhttps://doi.org/10.1172/JCI112072
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