Abstract
A high oxygen affinity hemoglobin, previously undescribed, was found in a healthy, asymptomatic patient with mild erythrocytosis and left-shifted hemoglobin-O2 dissociation curve. The hemoglobin variant could not be distinguished from Hb A by any of several electrophoretic methods nor by ion exchange chromatography. It was separated and analyzed by reversed phase high performance liquid chromatography. Structural analysis revealed the substitution beta 109 (G11) Val----Leu. The variant was named Hb Johnstown. The amino acid substitution perhaps disrupts alpha 1 beta 1 contacts in the deoxyhemoglobin conformation, thus shifting the equilibrium towards the high affinity oxyhemoglobin conformation.
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