Characterization of hemoglobin Burke [beta 107 (G9) Gly replaced by Arg].
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.
D000328:Adult; D000595:Amino Acid Sequence; D000743:Anemia, Hemolytic / Q000097:blood; D001120:Arginine; D001797:Blood Protein Electrophoresis; D004355:Drug Stability; D004588:Electrophoresis, Cellulose Acetate; D005260:Female; D005998:Glycine; D006455:Hemoglobins, Abnormal; D006801:Humans; D006863:Hydrogen-Ion Concentration; D010100:Oxygen / Q000097:blood
D006455:Hemoglobins, Abnormal; D001120:Arginine; D010100:Oxygen; D005998:Glycine