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Title: The isolation of lectins on acid-treated agarose. Author: Allen HJ, Johnson EA. Journal: Carbohydr Res; 1976 Aug; 50(1):121-31. PubMed ID: 10082. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]