Binding of indapamide to serum proteins and erythrocytes.

Article Details

Citation

Urien S, Riant P, Renouard A, Coulomb B, Rocher I, Tillement JP

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.

PubMed ID
3395370 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Drugs
Drug Carriers
DrugCarrierKindOrganismPharmacological ActionActions
Indapamidealpha1-acid glycoprotein (Protein Group)Protein groupHumans
Unknown
Binder
Details
IndapamideErythrocyteGroupHumans
Unknown
Binder
Details
IndapamideSerum albuminProteinHumans
Unknown
Binder
Details