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.
D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity / Q000379:methods; D003488:Cyanogen Bromide; D006020:Glycopeptides / Q000302:isolation & purification*; D008358:Mannose; D009844:Oligosaccharides / Q000302:isolation & purification; D011043:Pokeweed Mitogens; D013552:Swine; D013954:Thyroglobulin / Q000032:analysis*
D006020:Glycopeptides; D009844:Oligosaccharides; D011043:Pokeweed Mitogens; D013954:Thyroglobulin; D003488:Cyanogen Bromide; D008358:Mannose