The isolation of lectins on acid-treated agarose.
The ability of several D-galactose and N-acetyl-D-galactosamine-binding lectins to bind to Sepharose was investigated. Lectins from soybean, Wistaria floribunda, Bauhinia purpurea alba, and Sophora japonica could be isolated by affinity chromatography on acid-treated Sepharose 6B. These lectins would not bind to untreated Sepharose 2B, 4B, and 6B. The binding of B. purpurea alba and S. japonica was temperature-dependent. The S. japonica lectin would bind only at high pH. Ricinus communis toxin also showed a temperature-dependence of binding; acid-treated Sepharose 6B was a better affinity support for the toxin than was untreated Sepharose 4B Lectins from lima bean, Dolichos biflorus, and kidney-bean phytohemagglutinin did not bind to Sepharose under any of the conditions studied.
D001665:Binding Sites; D002846:Chromatography, Affinity; D002847:Chromatography, Agarose; D006863:Hydrogen-Ion Concentration; D037102:Lectins / Q000302:isolation & purification*; D008970:Molecular Weight; D037121:Plant Lectins; D010947:Plants, Toxic; D011485:Protein Binding; D012278:Ricinus; D013045:Species Specificity
D037102:Lectins; D037121:Plant Lectins