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Hemoglobin Saverne: A new variant with elongated β chains: Structural and functional properties

Hemoglobin, ISSN: 0363-0269, Vol: 12, Issue: 4, Page: 337-352
1988
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Article Description

A 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. © 1988 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.

Bibliographic Details

J. Delanoe-Garin; Y. Blouquit; N. Arous; J. Bardakdjian; C. Lacombe; J. Rosa; F. Galacteros; J. Kister; C. Poyart; M. L. North

Informa UK Limited

Medicine; Biochemistry, Genetics and Molecular Biology

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