Hemoglobin Saverne: A New Variant with Elongated β Chains: Structural and Functional Properties
1988; Taylor & Francis; Volume: 12; Issue: 4 Linguagem: Inglês
10.3109/03630268808998034
ISSN1532-432X
AutoresJ. Delanoe‐Garin, Y. Blouquit, N. Arous, J. Kister, Claire Poyart, M. L. North, J. Bardakdjian, C. Lacombe, J. Rosa, F. Galactéros,
Tópico(s)Erythrocyte Function and Pathophysiology
ResumoA 26-year-old French woman born in Saverne (France) was found to have Heinz body hemolytic anemia. Isoelectrofocusing showed the presence of an abnormal band amounting to 35% of the total hemoglobin concentration, suggesting a β variant. Structural analysis of the abnormal β chain showed an elongated C-terminal segment. Histidine 143 is replaced by a proline and the C-terminal sequence is identical to the corresponding segment of Hb Cranston. This new variant, named Hb Saverne, has β chains composed of 156 amino acid residues. Studies of its functional properties showed that Hb Saverne is an unstable, high affinity variant with low cooperativity.
Referência(s)