Biochem Genet. 1976 Aug;14(7-8):577-85.

Characterization of hemoglobin Burke [beta 107 (G9) Gly replaced by Arg].

Turner JW Jr, Jones RT, Brimhall B, DuVal MC, Koler RD.

Abstract

Hb Burke [beta 107 (G9) Gly replaced by Arg] was discovered in a young woman with hemolytic anemia. A substitution in this position has not been previously reported either in the human beta-chain or in any of the animal beta-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.

PMID:: 10883; [PubMed - indexed for MEDLINE]

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