Article
Isolated Hb Providence β82Asn and β82Asp fractions are more stable than native HbA(0) under oxidative stress conditions.
Biochemistry - 15 Nov 2011
Abraham Bindu, Hicks Wayne, Jia Yiping, Baek Jin Hyen, Miller Jeffery L, Alayash Abdu I
Abstract excerpt
We have previously shown that hydrogen peroxide (H(2)O(2)) triggers irreversible oxidation of amino acids exclusive to the β-chains of purified human hemoglobin (HbAo). However, it is not clear, whether α- or β-subunit Hb variants exhibit different oxidative resistance to H(2)O(2) when compared to their native HbAo. Hb Providence contains two β-subunit variants with single amino acid mutations at βLys82→Asp...
Topics
- Amino Acid Sequence
- Amino Acid Substitution
- Cyclic N-Oxides
- Cysteic Acid
- Dimerization
- Globins
- Heme
- Hemoglobin A
- Hemoglobin J
- Humans
- In Vitro Techniques
- Kinetics
- Models, Molecular
- Molecular Sequence Data