Article
Structural, functional, and subunit assembly properties of hemoglobin Attleboro [alpha 138 (H21) Ser----Pro], a variant possessing a site maturation at a critical C-terminal residue.
Biochemistry - 9 Jan 1990
McDonald M J, Michalski L A, Turci S M, Guillette R A, Jue D L, Johnson M H, Moo-Penn W F
Abstract excerpt
Hemoglobin Attleboro, a new alpha-chain variant with a substitution of proline for serine at position 138 (H21), was found to be a noncooperative high-affinity hemoglobin (P50 = 0.26 mmHg at pH 7 and 20 degrees C) which lacked an alkaline Bohr effect. Addition of 2,3-diphosphoglycerate (DPG) or i...
Topics
- Amino Acid Sequence
- Child, Preschool
- Female
- Hemoglobins, Abnormal
- Humans
- Ligands
- Macromolecular Substances
- Molecular Sequence Data
- Molecular Structure
- Mutation
- Oxygen
- Oxyhemoglobins
- Postural Balance
- Proline
- Protein Binding
- Serine