[Erythrocytosis due to a high-affinity hemoglobulin: mutant hemoglobin Saint-Jacques beta 140 (H18) Ala----Thr with a change in the 2,3-diphosphoglycerate binding site].

Abstract

All the high oxygen affinity variants have substitutions in regions that are crucial to hemoglobin function: mainly the alpha 1 beta 2 interface, the C-terminal end of the beta chain and the aminoacid residues involved in the 2,3 disphophoglycerate (2,3 DPG) binding site. In this report we describe a new variant with familial erythrocytosis: hemoglobin… (More)

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@article{Rochette1984ErythrocytosisDT, title={[Erythrocytosis due to a high-affinity hemoglobulin: mutant hemoglobin Saint-Jacques beta 140 (H18) Ala----Thr with a change in the 2,3-diphosphoglycerate binding site].}, author={Julie Rochette and J. P. Boissel and Dominique Labie and Henri Wajcman and Claire Poyart and Barbara Bohn and B. Varet}, journal={Nouvelle revue francaise d'hematologie}, year={1984}, volume={26 2}, pages={75-7} }