Abstract
Oxygen binding to isolated hemoglobin β SH chains exhibits heterotropic interactions with H +, inositol hexaphosphate and CO 2 which implies different structures of the liganded and unliganded β chains. In order to find out if the dissociation behaviour of β 4 SH homotetramers is likewise linked to oxygenation, we have measured the oxygen affinity of the pigment as a function of the protein concentration at different pH values. We found that a decrease in protein concentration is associated with a decrease in oxygen affinity. This result accords with predictions reached from studies on the self-association of liganded and unliganded β chains. Furthermore, it was established that both at high and low protein concentrations the oxygen affinity of the β chains is pH dependent.
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