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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

E ChianconeJ Wyman

PMID: 236

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

Hydrogen-Ion Concentration
Mathematics
Peptide Fragments
Phytin
Plasma Protein Binding Capacity
Protein Conformation
Carbon Monoxide
Carboxypeptidase
Chloride Ion Level
In Vivo NMR Spectroscopy
Paper Details
References
  • References10
  • Citations33
1
  • References10
  • Citations33
1234

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

European Journal of Biochemistry

Jul 1, 1975

E ChianconeJ 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

Hydrogen-Ion Concentration
Mathematics
Peptide Fragments
Phytin
Plasma Protein Binding Capacity
Protein Conformation
Carbon Monoxide
Carboxypeptidase
Chloride Ion Level
In Vivo NMR Spectroscopy

Related Papers

Paper Details
References
  • References10
  • Citations33
1
  • References10
  • Citations33
1234
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