Article

Biochemical Genetics

, Volume 14, Issue 7, pp 577-585

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

  • James W. TurnerJr.Affiliated withThe Springfield Plaza Professional Building
  • , Richard T. JonesAffiliated withDepartment of Biochemistry, University of Oregon Health Sciences Center
  • , Bernadine BrimhallAffiliated withDepartment of Biochemistry, University of Oregon Health Sciences Center
  • , Michael C. DuValAffiliated withDivision of Medical Genetics, University of Oregon Health Sciences Center
  • , Robert D. KolerAffiliated withDivision of Medical Genetics, University of Oregon Health Sciences Center

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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 Burke variant hemoglobin unstable hemoglobin