Nachbar M S, Oppenheim J D, Aull F
Biochim Biophys Acta. 1976 Feb 6;419(3):512-29. doi: 10.1016/0005-2736(76)90262-5.
Several aspects of the interaction of various lectins with the surface of Ehrlich ascites carcinoma cells are described. The order of agglutinating activity for various lectins is Ricinus communis greater than wheat germ greater than or equal to concanavalin A greater than or equal to soybean greater than Limulus polyphemus. No agglutination was noted for Ulex europaeus. Using 125I-labeled lectins it was determined that there are 1.6 and 7 times as many Ricinus communis lectin binding sites for concanavalin A and soybean lectins. Sodium deoxycholate-solubilized plasma membrane material was subjected to lectin affinity chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The lectin receptors of the plasma membrane appeared to be heterogeneous and some qualitative differences could be discerned among the electrophoretically analyzed material, which bound to and was specifically eluted from the various lectin affinity columns. The characteristics of elution of bound material from individual lectin columns indicated secondary hydrophobic interactions between concanavalin A or wheat germ agglutinin and their respective lectin receptor molecules.
本文描述了多种凝集素与艾氏腹水癌细胞表面相互作用的几个方面。各种凝集素的凝集活性顺序为：蓖麻凝集素＞麦胚凝集素≥伴刀豆球蛋白A≥大豆凝集素＞鲎凝集素。荆豆凝集素未观察到凝集现象。使用125I标记的凝集素确定，蓖麻凝集素结合位点的数量是伴刀豆球蛋白A和大豆凝集素结合位点数量的1.6倍和7倍。用脱氧胆酸钠增溶的质膜材料进行凝集素亲和层析和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳。质膜的凝集素受体似乎是异质性的，在电泳分析的与各种凝集素亲和柱结合并被特异性洗脱的材料中，可以看出一些定性差异。从各个凝集素柱上洗脱结合物质的特性表明，伴刀豆球蛋白A或麦胚凝集素与其各自的凝集素受体分子之间存在二级疏水相互作用。
