Recombinant hemoglobin(α29leucine → phenylalanine, α96valine → tryptophan, β108sparagine → lysine) exhibits low oxygen affinity and high cooperativity combined with resistance to autoxidation

Biochemistry

Volumn 38, Issue 40, 1999, Pages 13433-13442

  Jeong, Seong Tae ^a,b   Ho, Nancy T ^a   Hendrich, Michael P ^a   Ho, Chien ^a  

^a CARNEGIE MELLON UNIVERSITY   (United States)

^b Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; HEMOGLOBIN A; LEUCINE; OXYGEN; PHENYLALANINE; TRYPTOPHAN; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; AUTOOXIDATION; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; GENE THERAPY; HEMOGLOBIN ANALYSIS; HUMAN; MUTATION; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ACTIVITY RELATION;

AMINO ACID SUBSTITUTION; ASPARAGINE; CARBON MONOXIDE; ELECTRON SPIN RESONANCE SPECTROSCOPY; HEME; HEMOGLOBINS; HUMANS; KINETICS; LEUCINE; LYSINE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; OXYGEN; OXYHEMOGLOBINS; PHENYLALANINE; PROTEIN BINDING; RECOMBINANT PROTEINS; TRYPTOPHAN; VALINE;

ESCHERICHIA COLI;

EID: 0032834006     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991271t     Document Type: Article

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