Allen A K
Department of Biochemistry, Charing Cross and Westminster Medical School, London, UK.
Biochim Biophys Acta. 1995 May 11;1244(1):129-32. doi: 10.1016/0304-4165(94)00210-o.
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.
通过在甲状腺球蛋白-琼脂糖柱上进行亲和层析,从斑叶疆南星(天南星科)块茎中纯化出一种凝集素。该凝集素不是糖蛋白,亚基分子量为14,600。它被N-乙酰乳糖胺(Galβ1,4GlcNAc)特异性抑制,但不被单糖、乳糖(Galβ1,4Glc)、乳糖-N-二糖1(Galβ1,3GlcNAc)或壳二糖(GlcNAcβ1,4GlcNAc)显著抑制。含有N-乙酰乳糖胺结构的去唾液酸糖蛋白是该凝集素更有效的抑制剂。这种凝集素应该是用于检测糖蛋白中N-乙酰乳糖胺基团的有用探针。