Deras I L, Kawasaki N, Lee Y C
Department of Biology, Johns Hopkins University, Baltimore, MD 21218, USA.
Carbohydr Res. 1998 Feb;306(4):469-71. doi: 10.1016/s0008-6215(97)10112-4.
Some larger high-mannose-type oligosaccharides bind very tightly to concanavalin A and are difficult to elute. We present conditions that permit the complete elution of compounds containing high-mannose type oligosaccharides from a popular concanavalin A-Sepharose that is commercially available. Europium-labeled Man9GlcNAc2Asn (N. Kawasaki and Y.C. Lee, Anal. Biochem., 250 (1997) 260-262), soybean agglutinin, and Eu(III)-labeled soybean agglutinin bound to concanavalin A-Sepharose were completely eluted with 1 M methyl alpha-D-mannopyranoside by allowing the column to stand in elution buffer, permitting the oligosaccharide or glycoprotein to slowly dissociate from the column.
一些较大的高甘露糖型寡糖与伴刀豆球蛋白A紧密结合，难以洗脱。我们提出了一些条件，可使含有高甘露糖型寡糖的化合物从市售的一种常用伴刀豆球蛋白A-琼脂糖中完全洗脱出来。通过让柱子在洗脱缓冲液中静置，使寡糖或糖蛋白从柱子上缓慢解离，用1M的α-D-甘露吡喃糖苷可将铕标记的Man9GlcNAc2Asn（N.川崎和Y.C.李，《分析生物化学》，250 (1997) 260 - 262）、大豆凝集素以及与伴刀豆球蛋白A-琼脂糖结合的铕(III)标记的大豆凝集素完全洗脱下来。
