• DOI:10.1159/000137955
• Corpus ID: 3314740

Multiple binding of bepridil in human blood.

@article{Albengres1984MultipleBO,
  title={Multiple binding of bepridil in human blood.},
  author={Edith Albengres and Sa{\"i}k Urien and J. F. Pognat and Jean Paul Tillement},
  journal={Pharmacology},
  year={1984},
  volume={28 3},
  pages={
          139-49
        }
}

• E. Albengres, S. Urien, +1 author J. Tillement
• Published 1 July 1984
• Biology, Medicine
• Pharmacology

Using radiolabelled bepridil, equilibrium dialysis experiments and direct ligand-binding studies were conducted to characterize the binding of bepridil to some human serum proteins, and to blood cells and platelets, respectively. Bepridil was bound to serum albumin with K = 26 +/- 1.6 X 10(3) mol-1 X 1, n = 1.07 +/- 0.04; to alpha 1-acid glycoprotein with K = 442 +/- 68 X 10(3) mol-1 X 1, n = 0.90 +/- 0.04; and with a lesser extent to lipoproteins and gamma-globulins. Bepridil, propranolol, quinidine and erythromycin were found to share the same site on alpha 1-acid glycoprotein. The binding of bepridil to both RBC and WBC was nonspecific with the following parameters: NK = 10.55 +/- 0.10 per 5 X 10(6) RBC/mm3 and NK = 0.34 +/- 0.01 per 10(3) WBC/mm3, whereas the binding to platelets was saturable with N = 10.97 +/- 1.06 mumol/l per 108 +/- 10(3) platelets/mm3 and K = 40 +/- 8 X 10(3) mol-1 X 1. The binding parameters were used to simulate the distribution of bepridil between serum proteins, blood cells and platelets over the therapeutic range and showed that serum albumin, alpha 1-acid glycoprotein and RBC were the major binding components.