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41.
Kuroda Yukihiro Kita Yoko Shibukawa Akimasa Nakagawa Terumichi 《Pharmaceutical research》2001,18(3):389-393
Purpose. To establish a clear understanding of the role of biantennary branching glycans and genetic variants of 1-acid glycoprotein (AGP) in enantioselective bindings of basic drug.
Methods. Human native AGP was separated using concanavalin A affinity chromatography into two subfractions, the unretained fraction (UR-AGP, defect of biantennary glycan) and the retained fraction (R-AGP, possessing biantennary glycan(s)). Imminodiacetate-copper (II) affinity chromatography was used to separate human native AGP into A variant and a mixture of F1 and S variants (F1*S variants). The mixed solutions of the (R)- or (S)-isomer of the model drugs (15 M disopyramide (DP) or 30 M verapamil (VER)) and 40 M of respective AGP species were subjected to high-performance frontal analysis/capillary electrophoresis (HPFA/CE) to determine the unbound drug concentrations.
Results. The unbound concentrations (Cu) of DP in UR-AGP solutions were lower than those in R-AGP solutions, whereas there was no significant difference in the enantiomeric ratios (Cu(R)/Cu(S)) of DP between UR- and R-AGP solutions. In case of genetic variant, the Cu(R)/Cu(S) values of DP in F1*S and A solutions were 1.07 and 2.37, respectively. On the other hand, the enantiomeric ratio of VER in F1*S and A variant solutions were 0.900 and 0.871, respectively.
Conclusions. The biantennary glycan structures are related to binding affinity of DP to AGP, but not responsible for the enantioselectivity. Genetic variants give significant effect on the enantioselectivity in DP binding, but not in VER binding. 相似文献
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Igari A Nakagawa T Moriki T Yamaguchi Y Matsumoto M Fujimura Y Soejima K Murata M 《Thrombosis research》2012,130(3):e79-e83