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

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 alpha-D-Manp-(1 leads to 2)-alpha-D-Manp-(1 leads to 2)-alpha-D-Manp-(1 leads to 3)-beta-D-Manp-(1 leads to 4)-beta-GlcpNAc-(1 leads to 4)-beta-GlcpNAc leads to Asn was essential for the binding of glycopeptides to a Pa-2-Sepharose column.