Enzymatic preparation of biotinylated naturally-occurring sialylglycan and its molecular recognition on a quartz-crystal microbalance.
A biotinylated sialylglycan was prepared enzymatically by endo-M, and binding behavior of an SSA lectin was studied on a different coverage of a sialylglycan-immobilized 27 MHz quartz-crystal microbalance (QCM).
Mori
Toshiaki
T
Department of Biomolecular Engineering and Frontier Collaborative Research Center, Tokyo Institute of Technology, 4259 Nagatsuda, Midori-ku, Yokohama 226-8501, Japan.
Sekine
Yoshimi
Y
Yamamoto
Kenji
K
Okahata
Yoshio
Y
D000581:Amidohydrolases / Q000737:chemistry*; D001710:Biotin / Q000031:analogs & derivatives* / Q000096:biosynthesis; D019921:Biotinylation; D002240:Carbohydrate Sequence; D006020:Glycopeptides / Q000737:chemistry*; D006031:Glycosylation; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / Q000737:chemistry* / Q000378:metabolism; D008832:Microchemistry / Q000379:methods; D008969:Molecular Sequence Data; D009089:Mucor; D009844:Oligosaccharides / Q000096:biosynthesis*; D037121:Plant Lectins / Q000737:chemistry; D054788:Ribosome Inactivating Proteins
D006020:Glycopeptides; D009844:Oligosaccharides; D037121:Plant Lectins; C050600:Sambucus nigra lectins; C504890:biotinylated hen's egg sialyl glycopeptide; C105646:sialylglycopeptide, egg yolk; D001710:Biotin; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D054788:Ribosome Inactivating Proteins; D000581:Amidohydrolases; C027530:glycine-N-acylase