[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].
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| 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 Saint-Jacques beta 140 (H18) Ala----Thr, whose main abnormality is a defect in organic phosphate binding in the central cavity between to two beta chains. This variant could not be separated from hemoglobin A by standard electrophoretic methods or by isoelectric focusing. The abnormal peptide was isolated by reverse-phase high performance liquid chromatography and the structural modification determined by manual sequencing micro-method. Functional studies on red blood cells as well as on stripped lysate showed increased oxygen affinity, normal Bohr effect, decreased heme-heme interaction and loss of the 2,3 DPG regulatory effect.
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| Authors | J Rochette, J P Boissel, D Labie, H Wajcman, C Poyart, B Bohn, B Varet |
| Journal | Nouvelle revue francaise d'hematologie (Nouv Rev Fr Hematol (1978)) Vol. 26 Issue 2 Pg. 75-7 ( 1984) Germany |
| Vernacular Title | Polyglobulie par hémoglobine à affinité augmentée: hémoglobine Saint-Jacques beta 140 (H18) Ala----Thr, mutant présentant une altération du site de fixation du 2,3-diphosphoglycérate. |
| PMID | 6546989 (Publication Type: Case Reports, English Abstract, Journal Article, Research Support, Non-U.S. Gov't) |
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