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
- 22Citations
- 1Captures
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- Citations22
- Citation Indexes22
- CrossRef22
- 22
- Captures1
- Readers1
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.
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