Article
Mutations of the betaN102 residue of HbA not only inhibit the ligand-linked T to Re state transition, but also profoundly affect the properties of the T state itself.
Biochemistry - 20 Feb 2007
Kwiatkowski Laura D, Hui Hilda L, Karasik Ellen, Colby Judith E, Noble Robert W
Abstract excerpt
The properties of three HbA variants with different mutations at the beta102 position, betaN102Q, betaN102T, and betaN102A, have been examined. All three are inhibited in their ligand-linked transition from the low affinity T quaternary state to the high affinity Re quaternary state. In the presence of inositol hexaphosphate, IHP, none of them exhibits cooperativity in the binding of oxygen. This is consistent...
Topics
- Amino Acid Substitution
- Aspartic Acid
- Carbon Monoxide
- Glycine
- Hemoglobin A
- Humans
- Kinetics
- Ligands
- Light
- Mutation
- Oxygen