Honda S, Suzuki S, Nitta T, Kakehi K
Faculty of Phamraceutical Sciences, Kinki University, Higashi-Osaka, Japan.
J Chromatogr. 1988 Apr 1;438(1):73-84. doi: 10.1016/s0021-9673(00)90234-6.
Concanavalin A (Con A) or wheat germ agglutinin (WGA) was immobilized on a silica-based support, and the chromatographic behaviours of a series of dansylated ovalbumin-derived glycopeptides on small columns of the resultant gels were compared. These columns had high contents of lectins, and allowed differentiation of these glycopeptides. This method was rapid and reproducible, and enabled sensitive detection of these fluorescent glycopeptides. The structural requirement of these glycopeptides to manifest affinity to the immobilized lectins is also discussed, based on binding constants obtained from their retention times.
将伴刀豆球蛋白A（Con A）或麦胚凝集素（WGA）固定在硅胶基载体上，并比较了一系列丹磺酰化卵清蛋白衍生糖肽在所得凝胶小柱上的色谱行为。这些柱子含有高含量的凝集素，能够区分这些糖肽。该方法快速且可重复，能够灵敏地检测这些荧光糖肽。基于从保留时间获得的结合常数，还讨论了这些糖肽与固定化凝集素表现出亲和力的结构要求。
