Roberts D D, Goldstein I J
Arch Biochem Biophys. 1983 Jul 15;224(2):479-84. doi: 10.1016/0003-9861(83)90235-7.
Binding of the hydrophobic ligands 1,8-anilinonaphthalenesulfonic acid (ANS) and 2,6-toluidinylnaphthalenesulfonic acid (TNS) to a variety of plant lectins was studied by lectin-induced alteration of the fluorescence spectra of the two ligands. With one exception, all legume lectins examined bound ANS, with affinity constants ranging from 10(3) to 10(4) M-1. Similar ANS binding was noted for some nonlegume lectins. Titration of the five isolectins from Phaseolus vulgaris with ANS indicated positive cooperative binding of ANS to the two isolectins E4 and E3L1. Titrations with TNS revealed high-affinity sites for this ligand in a number of lectins. Addition of haptenic sugars did not inhibit binding of ANS, suggesting that the hydrophobic binding sites of lectins are independent of the carbohydrate binding sites.
通过凝集素诱导的两种配体荧光光谱变化，研究了疏水配体1,8 - 苯胺基萘磺酸（ANS）和2,6 - 甲苯胺基萘磺酸（TNS）与多种植物凝集素的结合情况。除一种情况外，所有检测的豆科凝集素均能结合ANS，其亲和常数范围为10³至10⁴ M⁻¹。一些非豆科凝集素也有类似的ANS结合情况。用ANS对菜豆的五种同工凝集素进行滴定，结果表明ANS与两种同工凝集素E4和E3L1存在正协同结合。用TNS滴定显示，许多凝集素中存在该配体的高亲和力位点。添加半抗原糖并不抑制ANS的结合，这表明凝集素的疏水结合位点与碳水化合物结合位点无关。
