title: Binding interactions of glycoproteins with lectins.
abstract: Since plant lectins were used to help define differences between normal and transformed cell surfaces (reviewed in References 1-4), they have been employed in many other situations where their sugar-recognition specificities could be used to advantage. One of these applications has been the purification and characterization of enzymes and other proteins; this work is reviewed here in order to define some of the variables that affect binding of glycoproteins to lectins, as well as to demonstrate how this technique has been profitably exploited for isolation of purified glycoproteins, and for their better understanding.
mesh_terms: D001667:Binding, Competitive; D002850:Chromatography, Gel; D003208:Concanavalin A; D004798:Enzymes / Q000302:isolation & purification; D006023:Glycoproteins / Q000378:metabolism*; D006027:Glycosides / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D037102:Lectins / Q000378:metabolism*; D009994:Osmolar Concentration; D013379:Substrate Specificity; D013696:Temperature; D013997:Time Factors
chemical_list: D004798:Enzymes; D006023:Glycoproteins; D006027:Glycosides; D037102:Lectins; D003208:Concanavalin A