Faye L, Salier J P
Université de Rouen, C.N.R.S. DO 203, Mont-Saint-Aignan, France.
Electrophoresis. 1989 Dec;10(12):841-7. doi: 10.1002/elps.1150101208.
In contrast to the conventional combination of physical, chemical and enzymatic methods used for a structural analysis of glycans in glycoproteins, alternative methods involve affinity electrophoresis as a tool for the detection, characterization, and quantitation of glycoproteins and their carbohydrate moiety, owing to interactions with lectins. Two major approaches involve (i) crossed affino-immunoelectrophoresis and variations thereof, whereby lectin/glycoprotein interactions occur during the electrophoretic runs, or (ii) affino-blotting, where the glycoproteins are electrophoretically separated and then immobilized onto a solid support prior to their interaction with lectins. A critical comparison of these two series of techniques is the scope of the present paper. These techniques are of high interest by virtue of their ability at differentiating a classical glycan structure from unusual oligosaccharide side chains. The former structures will usually be qualitatively and quantitatively described with the easy and fast procedures as well as the simple equipment required for crossed affino-immunoelectrophoresis or affino-blotting, whereas the latter will be good candidates for further structural analyses.
与用于糖蛋白聚糖结构分析的物理、化学和酶促方法的传统组合不同，替代方法涉及亲和电泳，作为检测、表征和定量糖蛋白及其碳水化合物部分的工具，这是由于其与凝集素的相互作用。两种主要方法包括：（i）交叉亲和免疫电泳及其变体，其中凝集素/糖蛋白相互作用在电泳过程中发生；或（ii）亲和印迹，其中糖蛋白先经电泳分离，然后在与凝集素相互作用之前固定在固体支持物上。对这两组技术进行批判性比较是本文的范围。这些技术因其能够区分经典聚糖结构与异常寡糖侧链而备受关注。前者的结构通常可以通过交叉亲和免疫电泳或亲和印迹所需的简便快速程序以及简单设备进行定性和定量描述，而后者则是进一步结构分析的良好候选对象。
