Bayard B, Kerckaert J P, Strecker G, Dorland L, van Halbeek H, Vliegenthart J F
Eur J Biochem. 1983 Dec 1;137(1-2):319-23. doi: 10.1111/j.1432-1033.1983.tb07831.x.
By affinity chromatography on concanavalin A (ConA) linked to Sepharose, S-carboxymethylated rat alpha-fetoprotein could be separated into two molecular variants: a ConA-reactive and a ConA-nonreactive fraction. The carbohydrate chains were quantitatively released from the protein by hydrazinolysis. Based on methylation analysis and high-resolution 1H-NMR spectroscopy of the re-N-acetylated hydrazinolysates, the carbohydrate structures of the two ConA-molecular variants of alpha-fetoprotein were established. The ConA-reactive species contains two N-glycosidic carbohydrate units per molecule, both having the following structure: (formula; see text) The ConA-nonreactive species possesses also two N-glycosidically linked oligosaccharide chains per molecule; each of these has the following structure: (formula; see text)
通过在与琼脂糖相连的伴刀豆球蛋白A（ConA）上进行亲和层析，S-羧甲基化大鼠甲胎蛋白可被分离为两种分子变体：一种与ConA反应，另一种不与ConA反应。通过肼解从蛋白质中定量释放出糖链。基于对重新N-乙酰化肼解产物的甲基化分析和高分辨率1H-NMR光谱，确定了甲胎蛋白两种ConA分子变体的糖结构。与ConA反应的变体每分子含有两个N-糖苷碳水化合物单元，两者均具有以下结构：（分子式；见正文）不与ConA反应的变体每分子也具有两条N-糖苷连接的寡糖链；每条链具有以下结构：（分子式；见正文）
