Glew R H, Doyle R J
Carbohydr Res. 1979 Aug;73:219-26. doi: 10.1016/s0008-6215(00)85491-9.
Concanavalin A is visibly aggregated by low concentrations of sodium dodecyl sulfate, maximum aggregation being obtained at pH 4.6. Other denaturants, such as urea, guanidine hydrochloride, Triton X-100, cetyltrimethylammonium bromide, Tween 80, and Brij 35 are ineffective in promoting visible aggregation. The sodium dodecyl sulfate-induced aggregation of concanavalin A requires the presence of an intact, saccharide-ligand binding-site. Rapid and complete reversal of the detergent effect was achieved by use of saccharides which bind to the lectin. Such compounds as tryptophan and o-nitrophenyl beta-D-galactopyranoside did not inhibit the aggregation of concanavalin A by sodium dodecyl sulfate, suggesting that the detergent does not bind the hydrophobic pocket on the surface of the protein. The results suggest that concanavalin A may have an additional, ligand-binding site which is metal-dependent and which can be modified by the addition of a saccharide ligand.
伴刀豆球蛋白A在低浓度十二烷基硫酸钠作用下会明显聚集，在pH 4.6时聚集程度最高。其他变性剂，如尿素、盐酸胍、Triton X-100、十六烷基三甲基溴化铵、吐温80和Brij 35，在促进可见聚集方面无效。十二烷基硫酸钠诱导的伴刀豆球蛋白A聚集需要完整的糖配体结合位点存在。通过使用与凝集素结合的糖类可实现去污剂效应的快速完全逆转。色氨酸和邻硝基苯基-β-D-吡喃半乳糖苷等化合物不抑制十二烷基硫酸钠诱导的伴刀豆球蛋白A聚集，这表明去污剂不与蛋白质表面的疏水口袋结合。结果表明，伴刀豆球蛋白A可能有一个额外的、依赖金属的配体结合位点，并且可以通过添加糖配体进行修饰。
