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

Biochemistry

Volumn 50, Issue 45, 2011, Pages 9752-9766

  Abraham, Bindu ^a   Hicks, Wayne ^a   Jia, Yiping ^a   Baek, Jin Hyen ^a   Miller, Jeffery L ^b   Alayash, Abdu I ^a  

^a CENTER FOR BIOLOGICS EVALUATION AND RESEARCH   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID ANALYSIS; DIMER FORMATION; INITIAL OXIDATION; IRREVERSIBLE OXIDATION; LIGAND BINDING; OXIDATION REACTIONS; OXIDATIVE PATHWAYS; OXIDATIVE REACTION; STRESS CONDITION; STRUCTURAL CHANGE; WILD TYPES;

AMINO ACIDS; FREE RADICAL REACTIONS; HYDROGEN PEROXIDE; REACTION RATES;

OXIDATION;

ASPARAGINE; ASPARTIC ACID; CYSTEIC ACID; CYSTEINE; HEMOGLOBIN A; HYDROGEN PEROXIDE;

AMINO ACID ANALYSIS; ARTICLE; ELECTROSPRAY MASS SPECTROMETRY; HUMAN; LIGAND BINDING; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MUTATIONAL ANALYSIS; OXIDATION; OXIDATIVE STRESS; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CYCLIC N-OXIDES; CYSTEIC ACID; DIMERIZATION; GLOBINS; HEME; HEMOGLOBIN A; HEMOGLOBIN J; HUMANS; 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;

EID: 80755156323     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200876e     Document Type: Article

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