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

✍ Scribed by Yasuhiro Katagiri; Kazuo Yamamoto; Tsutomu Tsuji; Toshiaki Osawa

• Publisher: Elsevier Science
• Year: 1983
• Tongue: English
• Weight: 675 KB
• Volume: 120
• Category: Article
• ISSN: 0008-6215
• DOI: 10.1016/0008-6215(83)88022-7

✦ Synopsis

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 a-D-Manp-( l-2)-cu-D-Manp-( l&2)-cY-D-Manp-( 1-3)~P-D-Manp-( 1-4)~P-GlcpNAc-( l-4)-&GlcpNAc+Asn was essential for the binding of glycopeptides to a Pa-2-Sepharose column.