Kinetics of the conformational changes of hemopexin in acid media.
Under the action of acid media the hemopexin molecule unfolds with resulting heme expulsion from the binding site, followed by heme dimerization and reassociation of dimeric heme with the unfolded protein molecule. The rate of the reaction is pH dependent and the whole process is fully reversible for a certain time interval. Prolonged treatment of hemopexin at acidic conditions, however, leads to the irreversible denaturation of this protein.
Kinetics of the conformational changes of hemopexin in acid media. Under the action of acid media the hemopexin molecule unfolds with resulting heme expulsion from the binding site, followed by heme dimerization and reassociation of dimeric heme with the unfolded protein molecule. The rate of the reaction is pH dependent and the whole process is fully reversible for a certain time interval. Prolonged treatment of hemopexin at acidic conditions, however, leads to the irreversible denaturation of this protein.