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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.
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