Centre de Recherches sur les Macromolécules Végétales C.N.R.S., B.P. 53X, F-38041, Grenoble Cedex, France.
Planta. 1991 Apr;184(1):8-13. doi: 10.1007/BF00208229.
A lectin specific for glucosamine oligomers has been purified by chitosan affinity chromatography from cultured cells of Rubus. The lectin, eluted by a glucosamine oligomer of degree of polymerization 4 in the presence of l-α-phosphatidylserine dipalmitoyl, was found by sodium dodecyl sulfate-polyacrylamide gel electroploresis to be homogeneous and to have a molecular weight of 67 kilodaltons; it could best bind the tetrasaccharide, as shown by ligand-blot processing. Data from kinetic-dependent enzyme-linked immunosorbent assays showed that the lectin has two apparent binding sites which better accommodate the tetrasaccharide and the hexasaccharide, respectively, of the glucosamineoligomer series. The affinity of the lectin for glucosamine oligomers was shown to decrease for chain lengths greater than six glucosaminyl residues.
一种特异性识别氨基葡萄糖低聚物的凝集素已通过几丁质亲和层析从悬培养的悬钩子属细胞中被分离纯化。这种凝集素在 l-α-磷脂酰丝氨酸二棕榈酰存在下,用聚合度为 4 的氨基葡萄糖低聚物洗脱,经十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析显示为均一的,分子量为 67 千道尔顿;通过配体印迹处理发现,它可以与四糖结合。动力学依赖性酶联免疫吸附测定的数据表明,该凝集素有两个明显的结合位点,分别更好地容纳氨基葡萄糖低聚物系列中的四糖和六糖。该凝集素对氨基葡萄糖低聚物的亲和力随链长大于六个氨基葡萄糖残基而降低。