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- W1570473786 abstract "Stereoselective human plasma protein binding of chlorpheniramine was studied by an ultrafiltration technique using a simple method of chiral stationary-phase liquid chromatographic resolution of racemic chlorpheniramine.The Scatchard plots of both chlorpheniramine enantiomers to human plasma protein showed high- and low-affinity components. Although there was no significant difference in the dissociation constant (Kd) between enantiomers at the high-affinity site, the Kd of (−)-chlorpheniramine in the low-affinity component was higher than that of (+)-chlorpheniramine. The number of binding sites (n2) of (+)- and (−)-chlorpheniramine in the low-affinity component were 24.4 and 25.0 nmol (mgprotein)−1, respectively. However, the partitioning constants (n/kd) of (+)-chlorpheniramine in the high- and low-affinity component were, respectively, approximately two-times higher than those of (−)-chlorpheniramine. Both (+)- and (−)-enantiomers appeared to bind to approximately one site per human serum α1-acid glycoprotein (HSAAG) molecule with a dissociation constant of 186.9 and 295.9 μM, respectively. Moreover, the binding to human serum albumin (HSA) of both enantiomers was weaker than that to HSAAG, and both enantiomers bound to approximately one site of HSA with a similar affinity.These results suggest that binding of (+)-chlorpheniramine to human plasma protein is stronger than that of (−)-chlorpheniramine, indicating a stereoselective binding of chlorpheniramine. The study also shows that the low affinity of binding of the enantiomers is in keeping with the AAG." @default.
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- W1570473786 date "1998-07-01" @default.
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- W1570473786 title "Stereoselective Binding of Racemic Chlorpheniramine to Human Plasma Protein" @default.
- W1570473786 doi "https://doi.org/10.1111/j.2042-7158.1998.tb00709.x" @default.
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