The estradiol-binding properties of the sheep haptoglobin-hemoglobin complex (Hp-Hb) have been studied. The time and temperature dependencies of the steroid binding have been established the tightly bound 17 beta-estradiol, which is not detached from the complex during precipitation or extraction, has been shown to form a part of the total amount of the steroid capable of bending to Hp-Hb. Disturbances in the protein-protein interactions between Hp and Hb lead to the dissociation of estradiol as well as to the loss by the protein of its estradiol-binding activity. The values of relative competitive activity for several steroids suggest that some structural elements of the 17 beta-estradiol molecule play a role in estradiol-protein interactions. It is assumed that the Hp-Hb complex has two or more 17 beta-estradiol binding sites.
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