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Identification of chloride-binding sites in hemoglobin by nuclear-magnetic-resonance quadrupole-relaxation studies of hemoglobin digests

European Journal of Biochemistry

Jul 1, 1975

Emilia ChianconeJ C Wyman

PMID: 236

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Abstract

35Cl minus-nuclear magnetic resonance (NMR) studies indicate that various digests of human hemoglobin with carboxypeptidase A and B, or a combination of the two, may be used for the identification of chloride binding sites. All the digestion products contain, like hemoglobin itself, at ...read more

Mentioned in this Paper

Phytin
Mathematics
Protein Conformation
Hydrogen-Ion Concentration
In Vivo NMR Spectroscopy
Eryhem
Peptide Fragments
Osmolality
Carbon Monoxide
Plasma Protein Binding Capacity
Paper Details
References
    • References7
    • Citations32
    • References7
    • Citations32
  • Identification of chloride-binding sites in hemoglobin by nuclear-magnetic-resonance quadrupole-relaxation studies of hemoglobin digests

    European Journal of Biochemistry

    Jul 1, 1975

    Emilia ChianconeJ C Wyman

    PMID: 236

    DOI:

    Abstract

    35Cl minus-nuclear magnetic resonance (NMR) studies indicate that various digests of human hemoglobin with carboxypeptidase A and B, or a combination of the two, may be used for the identification of chloride binding sites. All the digestion products contain, like hemoglobin itself, at ...read more

    Mentioned in this Paper

    Phytin
    Mathematics
    Protein Conformation
    Hydrogen-Ion Concentration
    In Vivo NMR Spectroscopy

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    Paper Details
    References
    • References7
    • Citations32
    • References7
    • Citations32
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