ONE-STEP PURIFICATION OF MURINE IGM AND HUMAN ALPHA-2-MACROGLOBULIN BY AFFINITY-CHROMATOGRAPHY ON IMMOBILIZED SNOWDROP BULB LECTIN
ONE-STEP PURIFICATION OF MURINE IGM AND HUMAN ALPHA-2-MACROGLOBULIN BY AFFINITY-CHROMATOGRAPHY ON IMMOBILIZED SNOWDROP BULB LECTIN
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DOI：
10.1016/0003-9861(88)90076-8
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发表时间：
1988-12-01
影响因子：
3.9
通讯作者：
GOLDSTEIN, IJ
中科院分区：
文献类型：
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作者：
SHIBUYA, N;BERRY, JE;GOLDSTEIN, IJ
从雪花莲鳞茎中分离到一种新的甘露糖特异性植物凝集素（GNA），将其固定在Sepharose 4 B上，并用于某些高甘露糖型糖链糖蛋白的纯化。鼠IgM与该柱紧密结合，并用0.1M甲基α-葡聚糖洗脱。D-甘露糖苷，而牛和鼠IgG不结合。当将含有IgM单克隆抗体的鼠杂交瘤血清加到该柱上时，用甲基α-葡聚糖洗脱后得到高度纯化的IgM抗体。D-甘露糖苷相反，人IgM不被该柱结合，尽管报道其含有高甘露糖型聚糖链。α 2-巨球蛋白是存在于人血清中的唯一糖蛋白，其被固定的雪花莲凝集素柱结合。似乎只有含有多个Man（α 1，3）Man单元的糖蛋白与固定的凝集素结合。
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.