Hemoglobin Saverne: a new variant with elongated beta chains: structural and functional properties

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 beta variant. Structural analysis of the abnormal beta chain showed an el...

Full description

Saved in:
Bibliographic Details
Published inHemoglobin Vol. 12; no. 4; p. 337
Main Authors Delanoe-Garin, J, Blouquit, Y, Arous, N, Kister, J, Poyart, C, North, M L, Bardakdjian, J, Lacombe, C, Rosa, J, Galacteros, F
Format Journal Article
LanguageEnglish
Published England 1988
Subjects
Adult
Amino Acid Sequence
Binding, Competitive
Female
Hemoglobins, Abnormal - analysis
Hemoglobins, Abnormal - genetics
Humans
Isoelectric Point
Mutation
Oxygen - blood
Peptide Mapping
Online AccessGet more information

Cover

More Information
Summary: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 beta variant. Structural analysis of the abnormal beta 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 beta 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.
ISSN:0363-0269
1532-432X
DOI:10.3109/03630268808998034