Prednisolone binding to albumin and transcortin in the presence of cortisol

Biochem Pharmacol. 1982 Feb 1;31(3):289-92. doi: 10.1016/0006-2952(82)90172-1.


The protein binding of prednisolone was assessed in a 5% albumin solution and in pooled human serum, alone and in the presence of various amounts of cortisol. Significant displacement of prednisolone from transcortin binding sites occurred with little or no change in transcortin binding capacity or affinity constant for prednisolone, suggesting competitive inhibition of prednisolone binding by cortisol. Little or no displacement of prednisolone from the protein binding sites on albumin occurred though a decrease in the number of binding sites (four vs two), and an increase in the affinity constant for the albumin-prednisolone interaction (4.32 X 10(2) vs 9.43 X 10(2) M-1) occurred in the presence of cortisol. Allosteric conformational changes may occur in albumin structure in the presence of cortisol. These alterations have no effect on the fraction of prednisolone bound to albumin.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Allosteric Regulation
  • Binding Sites
  • Binding, Competitive
  • Humans
  • Hydrocortisone / metabolism*
  • In Vitro Techniques
  • Kinetics
  • Prednisolone / metabolism*
  • Protein Binding
  • Serum Albumin / metabolism*
  • Transcortin / metabolism*


  • Serum Albumin
  • Transcortin
  • Prednisolone
  • Hydrocortisone