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

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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.

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Authors and Affiliations

  1. The Springfield Plaza Professional Building, Springfield, Virginia

    James W. Turner Jr.

  2. Department of Biochemistry, University of Oregon Health Sciences Center, 97201, Portland, Oregon

    Richard T. Jones & Bernadine Brimhall

  3. Division of Medical Genetics, University of Oregon Health Sciences Center, Portland, Oregon

    Michael C. DuVal & Robert D. Koler

Authors
  1. James W. Turner Jr.
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  2. Richard T. Jones
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  3. Bernadine Brimhall
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  4. Michael C. DuVal
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  5. Robert D. Koler
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Additional information

This work was supported in part by U.S. Public Health Service Grants AM-17850 and AM-18006.

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Turner, J.W., Jones, R.T., Brimhall, B. et al. Characterization of hemoglobin Burke [β107 (G9) Gly→Arg]. Biochem Genet 14, 577–585 (1976). https://doi.org/10.1007/BF00485836

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  • DOI: https://doi.org/10.1007/BF00485836

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