A new hemoglobin variant altering the α1β2 contact: Hb Chemilly α2β2 99(G1)Asp→Val

FEBS Letters

Varet, B.³  Poyart, C.²  Wajcman, H.¹  Rochette, J.¹ 

[1] Institut de Pathologie et Biologie Cellulaires et Moléculaires, INSERM U.15, 24 rue du Fg St-Jacques, 75014 Paris, France;INSERM U.27, 42 rue Desbassayns de Richemont, 92150 Suresnes, France;Département d'Hématologie CHU COCHIN, 25 rue du Fg St-Jacques, 75014, Paris, France

关键词: Hb variant;    Erythrocytes;    Oxygen affinity;    Reversed phase HPLC;   

DOI  :  10.1016/0014-5793(84)80034-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Hemoglobin Chemilly (α₂β₂ 99(G1)Asp→Val), a high oxygen affinity variant, was uncovered in the red blood cells of a polycythemic patient who reported to the hospital concerning periodic headaches. We describe the molecular abnormality and functional studies of this new abnormal Hb. β 99(G1)Asp, an invariant residue of hemoglobin, is considered a key amino acid for conformational changes between the R⇆T quaternary structures responsible for the allosteric behavior of hemoglobin. Hb Chemilly exhibits a high 0₂ affinity, very low cooperativity and reduced Bohr effect. Its functional abnormalities are compared to the 5 other Hb variants at site β 99(G1) described up to now of the 7 single base substitutions predictable from the genetic code.

【 授权许可】

Unknown