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

Hemoglobin. 1988;12(4):337-52. doi: 10.3109/03630268808998034.

Abstract

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.

Publication types

  • Case Reports
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Amino Acid Sequence
  • Binding, Competitive
  • Female
  • Hemoglobins, Abnormal / analysis*
  • Hemoglobins, Abnormal / genetics
  • Humans
  • Isoelectric Point
  • Mutation*
  • Oxygen / blood
  • Peptide Mapping

Substances

  • Hemoglobins, Abnormal
  • hemoglobin Saverne
  • Oxygen