Abstract
The binding of cocaine (COC) and cocaethylene (CE) in human serum was studied by equilibrium dialysis. Scatchard analysis suggested a high-affinity binder (Ka, 2.56 × 104 L/mol; Bo, 7.38 × 10−5 mol/L) and a low-affinity binder (Ka, 4.47 × 103 L/mol; Bo, 2.77 × 10−4 mol/L) for COC. Two high-affinity binders (Ka, 5.21 × 104 L/mol; Bo, 2.54 × 10−5 mol/L; and Ka, 4.32 × 104 L/mol; Bo, 2.43 × 10−5 mol/L) were discernible for CE. For both compounds additional, very-low-affinity, highcapacity (nonspecific) binding was also seen. Supplementation of serum with specific proteins suggested that the high-affinity binding was due to alpha-1-acid glycoprotein, whereas the low-affinity binding was due to albumin, inasmuch as such supplementation increased the ratio of bound to free drug for both COC and CE.

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