Oxygen-Equilibrium Characteristics of Hemoglobin Norfolk (α^57Asp₂β^A₂)

Abstract

Oxygen-equilibrium characteristics of Hb Norfolk (α^57Asp₂β^A₂) are shown to be identical with those of Hb A. The amino acid substitution occurred in the position E6 (α57) which is adjacent to the distal histidine residue• in the primary structure of the mutant hemoglobin does not produce any measurable effect on the functional property of heme iron. The structure-function relationships of the substituted side chain are briefly discussed.