Binding of indapamide to serum proteins and erythrocytes.
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.
Urien
S
S
Laboratoire de Pharmacologie, Faculté de Médecine, Créteil, France.
Riant
P
P
Renouard
A
A
Coulomb
B
B
Rocher
I
I
Tillement
J P
JP
D001792:Blood Platelets / Q000378:metabolism; D001798:Blood Proteins / Q000378:metabolism*; D004232:Diuretics / Q000493:pharmacokinetics*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007190:Indapamide / Q000493:pharmacokinetics*; D008074:Lipoproteins / Q000378:metabolism; D009961:Orosomucoid / Q000378:metabolism; D012709:Serum Albumin / Q000378:metabolism
D001798:Blood Proteins; D004232:Diuretics; D008074:Lipoproteins; D009961:Orosomucoid; D012709:Serum Albumin; D007190:Indapamide