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J Steroid Biochem. 1983 Jul;19(1A):1-15.

Steroid-protein interaction: from past to present.


In this review, the association between biologically active compounds and proteins is seen in the light of axioms expressed by Paracelsus and Paul Ehrlich long ago, and the physiological significance of the interactions is pointed out. Of the various types of proteins that form noncovalent complexes with steroid hormones, only the serum proteins will be discussed. Recent results, obtained in several laboratories, on the physicochemical properties of the human corticosteroid-binding globulin (CBG, transcortin) makes this glycoprotein perhaps the best known one among the steroid-binding serum proteins. Influence of pH on stability of the complexes, kinetics of the associations and their significance, as well as thermodynamic parameters of complex formation are being discussed. Characteristics of the binding sites are deduced from specificity studies. Influence of the entrance of hydrophilic or hydrophobic substituents into the steroid molecule illuminates the difference between typically hydrophobic binders such as the progesterone-binding globulin (PBG) of the pregnant guinea-pig and typically hydrophilic binders such as CBG. Complete elucidation of the steroid-binding proteins awaits the determination of the amino acid sequence and the X-ray crystallographic analysis of the steroid-protein complex.

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