PURIFICATION AND CHARACTERIZATION OF AN N-ACETYLLACTOSAMINE-SPECIFIC LECTIN FROM TUBERS OF ARUM-MACULATUM
PURIFICATION AND CHARACTERIZATION OF AN N-ACETYLLACTOSAMINE-SPECIFIC LECTIN FROM TUBERS OF ARUM-MACULATUM
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DOI：
10.1016/0304-4165(94)00210-o
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发表时间：
1995-05-11
影响因子：
3
通讯作者：
ALLEN, AK
中科院分区：
文献类型：
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作者：
ALLEN, AK
用甲状腺球蛋白-琼脂糖凝胶柱亲和层析法从天南星科植物斑叶天南星的块茎中分离纯化了一种凝集素。凝集素不是糖蛋白，亚基分子量为14600。它被N-乙酰乳糖胺（Gal β 1，4GlcNAc）特异性抑制，但不被单糖或乳糖（Gal β 1，4Glc）、乳糖-N-二糖1（Gal β 1，3GlcNAc）或壳二糖（GlcNAc β 1，4GlcNAc）显著抑制。含有N-乙酰乳糖胺结构的去唾液酸糖蛋白是甚至更有效的凝集素抑制剂。这种凝集素应该是一个有用的探针N-乙酰乳糖胺基团的糖蛋白。
A lectin was purified from the tubers of Arum maculatum (family Araceae) by affinity chromatography on a thyroglobulin-Sepharose column. The lectin is not a glycoprotein and has a subunit molecular weight of 14 600. It is specifically inhibited by N-acetyllactosamine (Gal beta 1,4GlcNAc), but is not significantly inhibited by monosaccharides or by lactose (Gal beta 1,4Glc), lacto-N-biose 1 (Gal beta 1,3GlcNAc), or chitobiose (GlcNAc beta 1,4GlcNAc). Asialoglycoproteins which contain N-acetyllactosamine structures are even more effective inhibitors of the lectin. This lectin should be a useful probe for N-acetyllactosamine groups in glycoproteins.