Article
Hemoglobin Dallas (alpha 97(G4)Asn-->Lys): functional characterization of a high oxygen affinity natural mutant.
Biochimica et biophysica acta - 13 Oct 1992
Lendaro E, Ippoliti R, Brancaccio A, Bellelli A, Vallone B, Ivaldi G, Sciarratta G V, Castello C, Tomova S, Brunori M
Abstract excerpt
Hemoglobin Dallas, an alpha-chain variant with a substitution of lysine for asparagine at position 97(G4), was found to have increased oxygen affinity (p1/2 = 1 mmHg at pH 7.3 and 20 degrees C), diminished cooperativity (n, the Hill coefficient = 1.7) and reduced Bohr effect (about 50%). Addition of allosteric effectors (such as 2,3-diphosphoglycerate, inositol hexakisphosphate and bezafibrate) led to a decrease...
Topics
- Allosteric Regulation
- Hemoglobins, Abnormal
- Humans
- Kinetics
- Models, Molecular
- Mutation
- Oxygen