Biochemical Genetics

, Volume 14, Issue 7, pp 577–585

Characterization of hemoglobin Burke [β107 (G9) Gly→Arg]

  • James W. TurnerJr.
  • Richard T. Jones
  • Bernadine Brimhall
  • Michael C. DuVal
  • Robert D. Koler
Article

DOI: 10.1007/BF00485836

Cite this article as:
Turner, J.W., Jones, R.T., Brimhall, B. et al. Biochem Genet (1976) 14: 577. doi:10.1007/BF00485836
  • 9 Views

Abstract

Hb Burke [β107 (G9) Gly→Arg] was discovered in a young woman with hemolytic anemia. A substitution in this position has not been previously reported either in the human β-chain or in any of the animal β-chains so far sequenced. The abnormal hemoglobin shows heat instability and a lowered oxygen affinity. The substitution of a large charged arginine residue for the small glycine residue in the G helix next to a heme contact (Leu-106) may be responsible for these effects. Hb Burke is compared with five other hemoglobins having Gly-Arg substitutions in other parts of the molecule.

Key words

Hb Burkevariant hemoglobinunstable hemoglobin

Copyright information

© Plenum Publishing Corporation 1976

Authors and Affiliations

  • James W. TurnerJr.
    • 1
  • Richard T. Jones
    • 2
  • Bernadine Brimhall
    • 2
  • Michael C. DuVal
    • 3
  • Robert D. Koler
    • 3
  1. 1.The Springfield Plaza Professional BuildingSpringfield
  2. 2.Department of BiochemistryUniversity of Oregon Health Sciences CenterPortland
  3. 3.Division of Medical GeneticsUniversity of Oregon Health Sciences CenterPortland