Structural requirements for the binding of high-mannose-type glycopeptides to immobilized pokeweed Pa-2 lectin

Abstract The structural requirements for the interaction of asparagine-linked glycopeptides with immobilized pokeweed mitogen Pa-2 were investigated. Some high-mannose-type glycopeptides obtained from porcine thyroglobulin were found to have strong affinity for Pa-2-Sepharose, whereas complex- and hybrid-type glycopeptides were shown to have much weaker affinity. The elution profiles of various glycopeptides modified by glycosidase treatment and acetolysis showed that the total structure α- d -Man p -(1→2)-α- d -Man p -(1→2)-α- d -Man p -(1→3)-β- d -Man p -(1→4)-β- Glc p NAc-(1→4)-β-Glc p NAc→Asn was essential for the binding of glycopeptides to a Pa-2-Sepharose column.