The role of branching glycan of human α1-acid glycoprotein in enantioselective binding to basic drugs as studied by capillary electrophoresis

被引：34

作者：

Kuroda, Y ^{[1
]}

Shibukawa, A ^{[1
]}

Nakagawa, T ^{[1
]}

机构：

[1] Kyoto Univ, Grad Sch Pharmaceut Sci, Sakyo Ku, Kyoto 6068501, Japan

来源：

ANALYTICAL BIOCHEMISTRY | 1999年 / 268卷 / 01期

关键词：

capillary electrophoresis; high-performance frontal analysis; propranolol; verapamil;

D O I：

10.1006/abio.1998.3050

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The role of the branching glycan structure of human alpha(1)-acid glycoprotein (AGP) in the interaction with basic drugs was investigated in terms of enantioselectivity in binding ability. AGP was separated by concanavalin A lectin affinity chromatography into two subfractions, the unretained AGP (UR-AGP) which has no biantennary glycan chain and the retained AGP (R-AGP) which possesses biantennary oligosaccharide chain(s). The unbound concentrations of propranolol (PRO) enantiomers and verapamil (VER) enantiomers in UR-AGP solution and R-AGP solution were determined by high-performance frontal analysis combined with capillary electrophoresis. It was found that (S)-PRO is bound to UR-AGP and R-AGP more strongly than (R)-PRO, whereas the reverse applies to VER enantiomers, and that such enantioselectivity is common to these proteins. This suggests that the branching type of glycan chains of AGP does not play significant role in the chiral recognition in binding these basic drugs. (C) 1999 Academic Press.

引用

页码：9 / 14

页数：6

共 28 条

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