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Digitale Medien

Characterization of hemoglobin Burke [β107 (G9) Gly→Arg] (1976)

Turner, James W. ; Jones, Richard T. ; Brimhall, Bernadine ; [weitere]

Springer

Biochemical genetics 14 (1976), S. 577-585

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Details

ISSN: 1573-4927

Schlagwort(e): Hb Burke ; variant hemoglobin ; unstable hemoglobin

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie , Chemie und Pharmazie

Notizen: 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.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00485836

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