Analysis of binding affinity of sugars to concanavalin A by surface plasmon resonance sensor BIACORE

被引：2

作者：

Goto, S

Terada, H

机构：

[1] Univ Tokushima, Fac Pharmaceut Sci, Tokushima 7708505, Japan

[2] Sci Univ Tokyo, Fac Pharmaceut Sci, Shinjuku Ku, Tokyo 1350024, Japan

来源：

SPECTROSCOPY-AN INTERNATIONAL JOURNAL | 2002年 / 16卷 / 3-4期

关键词：

D O I：

10.1155/2002/814658

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The observed dissociation constant k(d) of the lectin concanavalin A (ConA) from glycoprotein asialofetuin (ASF) changed with the concentration of inhibitory sugars. The reciprocal of k(d) showed a linear relationship with the reciprocal of sugar concentration. This regression line was found to be theoretically available in the analysis of the kinetics in the interaction of sugars with ConA under conditions where the binding constant K-i of sugars to ConA is more than about 333.

引用

页码：285 / 288

页数：4

共 3 条

[1] PROTEIN-CARBOHYDRATE INTERACTION .2. INHIBITION STUDIES ON INTERACTION OF CONCANAVALIN A WITH POLYSACCHARIDES [J].