Binding of indapamide to serum proteins and erythrocytes

Biochem Pharmacol. 1988 Aug 1;37(15):2963-6. doi: 10.1016/0006-2952(88)90282-1.


The binding of indapamide to isolated serum proteins and erythrocytes was studied in order to understand its blood distribution. In serum, indapamide was mainly bound to alpha 1-acid glycoprotein with a high affinity (K = 73.4/mM), and to albumin and lipoproteins. Indapamide was bound to erythrocytes via a saturable process with a high affinity (K = 385/mM and N = 57 microM for an hematocrit value of 0.48), and erythrocytes were the main binding component in blood (more than 80% of indapamide was associated to erythrocytes in blood). The binding to serum proteins affected indapamide distribution in blood, and alpha 1-acid glycoprotein was shown to be the more effective protein in decreasing the amount of indapamide associated to erythrocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blood Platelets / metabolism
  • Blood Proteins / metabolism*
  • Diuretics / pharmacokinetics*
  • Erythrocytes / metabolism*
  • Humans
  • In Vitro Techniques
  • Indapamide / pharmacokinetics*
  • Lipoproteins / metabolism
  • Orosomucoid / metabolism
  • Serum Albumin / metabolism


  • Blood Proteins
  • Diuretics
  • Lipoproteins
  • Orosomucoid
  • Serum Albumin
  • Indapamide