Shibuya N, Berry J E, Goldstein I J
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109.
Arch Biochem Biophys. 1988 Dec;267(2):676-80. doi: 10.1016/0003-9861(88)90076-8.
A new mannose-specific plant lectin (GNA) isolated from the snowdrop bulb was immobilized on Sepharose 4B and employed for the purification of certain glycoproteins with high-mannose type glycan chains. Murine IgM bound tightly to this column and was eluted with 0.1 M methyl alpha-D-mannoside whereas bovine and murine IgG were not bound. When a murine hybridoma serum containing IgM monoclonal antibody was applied to this column, highly purified IgM antibody was obtained after elution with methyl alpha-D-mannoside. On the contrary, human IgM was not bound by this column despite reports that it contains high-mannose type glycan chains. alpha 2-Macroglobulin was the sole glycoprotein present in human serum which was bound by the immobilized snowdrop lectin column. It appears that only glycoproteins containing multiple Man(alpha 1,3)Man units are bound to the immobilized lectin.
从雪花莲鳞茎中分离出的一种新的甘露糖特异性植物凝集素（GNA）被固定在琼脂糖4B上，用于纯化某些带有高甘露糖型聚糖链的糖蛋白。鼠IgM与该柱紧密结合，并用0.1Mα-D-甲基甘露糖苷洗脱，而牛IgG和鼠IgG则不结合。当将含有IgM单克隆抗体的鼠杂交瘤血清应用于该柱时，用α-D-甲基甘露糖苷洗脱后可获得高度纯化的IgM抗体。相反，尽管有报道称人IgM含有高甘露糖型聚糖链，但它不与该柱结合。α2-巨球蛋白是人类血清中唯一能与固定化雪花莲凝集素柱结合的糖蛋白。似乎只有含有多个Man（α1,3）Man单元的糖蛋白才能与固定化凝集素结合。
