Binding of antiarrhythmic drugs to purified human alpha 1-acid glycoprotein.

The binding of lidocaine, verapamil, propafenone and propranolol to isolated, purified human alpha 1-acid glycoprotein was studied using equilibrium dialysis. Lidocaine and verapamil bound to a single class of binding sites which was characterized by high affinity (kd1 for lidocaine was 5.79 x 10(-6)M-1 and for verapamil 3.43 X 10(-6)M-1) and low capacity (n = 0.40 for lidocaine and 0.62 for verapamil). The binding of propafenone revealed two classes of binding sites, both with high affinity (kd1 was 7.62 X 10(-6)M-1 and kd2 was 6.00 X 10(-8)M-1) and low capacity (n1 = 0.79 and n2 = 0.20). Propranolol bound to at least two classes of binding sites (kd1 was 2.56 X 10(-6)M-1; n1 = 0.58). Complete characterization of the binding parameters of the second site was not possible due to failure to achieve saturation.