Jacalin interacts with Asn‐linked glycopeptides containing multi‐antennary oligosaccharide structure with terminal α‐linked galactose

FEBS Letters

Lee, Ki-Young¹  Do, Su-Il¹ 

[1] Korea Research Institute of Bioscience and Biotechnology (KRIBB), Animal Cell and Medical Glycobiology Laboratory, Molecular Glycobiology Research Unit, P.O. Box 115, Yusung, Taejon 305-600, South Korea

关键词: Jacalin lectin;    RAF9 cell-derived N-linked glycopeptide;    Terminal α-galactose residue;    α-Galactosidase;    CHO;    Chinese hamster ovary;    N-linked;    asparagine-linked;    O-linked;    serine/threonine-linked;    Con A;    concanavalin A;    GlcNAc;    N-acetylglucosamine;    GalNAc;    N-acetylgalactosamine;    a-m-gal;    α-methylgalactopyranoside;    a-m-glc;    α-methylglucoside;    a-m-man;    α-methylmannoside;    BSA;    bovine serum albumin;   

DOI  :  10.1016/S0014-5793(97)01539-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The carbohydrate binding properties of jacalin lectin were examined using RAF9 cell-derived d-[6-³H]glucosamine-radiolabeled total glycopeptides containing N-linked and O-linked oligosaccharides. The binding of N-linked glycopeptides to jacalin was abolished by treatment of α-galactosidase whereas O-linked glycopeptides were still bound lectin after this treatment. The removal of O-linked oligosaccharides by mild alkaline/borohydride treatment completely eliminated the lectin binding of α-galactosidase treated glycopeptides. These results demonstrate that jacalin interacts with cellular glycopeptides containing N-linked oligosaccharides with terminal α-galactose residues as well as glycopeptides containing O-linked oligosaccharides.

【 授权许可】

Unknown