[Study of hemoglobin structure using the allosteric label method]

Abstract

The rate of human hemoglobin oxidation in the presence of various sulfhydryl reagents essentially depends on the degree of binding of different sulfhydryl groups of hemoglobin during the oxidation process. Kinetics of modified hemoglobin oxidation is biphasic, which allows to judge the effect of reagent-hemoglobin binding on the state of rapidly and slowly oxidated subunits separately.