Improved separation at low temperature of glycoproteins by Con A-Sepharose affinity chromatography in the presence of sodium dodecyl sulfate (SDS).
The Con A-Sepharose affinity chromatography of glycoproteins was even more effective at 4 degrees C than that at room temperature (26-28 degrees C) in the presence of sodium dodecyl sulfate (SDS). Application of this methodology to the separation of several glycoproteins from SDS-solubilized membrane proteins in rat cerebellum, including a glycoprotein characteristic of the Purkinje cells, was successful.
D000818:Animals; D002462:Cell Membrane / Q000032:analysis; D002531:Cerebellum / Q000032:analysis; D002846:Chromatography, Affinity / Q000379:methods*; D003080:Cold Temperature; D003208:Concanavalin A; D006023:Glycoproteins / Q000302:isolation & purification*; D009419:Nerve Tissue Proteins / Q000302:isolation & purification; D051381:Rats; D012967:Sodium Dodecyl Sulfate
D006023:Glycoproteins; D009419:Nerve Tissue Proteins; D003208:Concanavalin A; D012967:Sodium Dodecyl Sulfate