$Isolated Hb Providence β82Asn and β82Asp fractions are more stable than native HbA(0) under oxidative stress conditions$

Isolated Hb Providence β82Asn and β82Asp fractions are more stable than native HbA(0) under oxidative stress conditions

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 t...

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Veröffentlicht in:	Biochemistry (Easton) 2011-11, Vol.50 (45), p.9752-9766
Hauptverfasser:	Abraham, Bindu, Hicks, Wayne, Jia, Yiping, Baek, Jin Hyen, Miller, Jeffery L, Alayash, Abdu I
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acid Substitution Cyclic N-Oxides Cysteic Acid - chemistry Dimerization Globins - chemistry Heme - chemistry Hemoglobin A - chemistry Hemoglobin A - genetics Hemoglobin A - metabolism Hemoglobin J - chemistry Hemoglobin J - genetics Hemoglobin J - metabolism Humans In Vitro Techniques Kinetics Models, Molecular Molecular Sequence Data Mutation Oxidative Stress Protein Stability Protein Structure, Quaternary Protein Subunits Spectrometry, Mass, Electrospray Ionization Spin Labels Tandem Mass Spectrometry
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