Abstract
Abstract
The plasma protein binding properties of the calcium channel blocker diltiazem were studied using a three-chamber equilibrium dialysis system. Diltiazem is 81% bound to human sera with significant inter-individual variation. The relative binding of diltiazem by lipoproteins and α1-acid glycoprotein was higher than by albumin. The binding to low density lipoprotein was strong and appeared not to be associated with the surface apoprotein.
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