[Structure of the carbohydrate chain of riboflavin-binding glycoprotein from hen egg white. Neutral oligosaccharides of the hybrid type].
Reductive cleavage of the riboflavin-binding glycoprotein from hen egg white with LiBH4/tert-BuOH followed by NaBH4 treatment gave rise to oligosaccharide alditols. After fractionation by HPLC two individual oligosaccharide alditols of a hybrid type were isolated. Their structures were proved by 1H NMR 500 MHz spectroscopy and methylation analysis. One of the oligosaccharides has earlier been found in ovalbumin, whereas the other is identified in glycoproteins for the first time.
Likhosherstov
L M
LM
Piskarev
V E
VE
Sepetov
N F
NF
Derevitskaia
V A
VA
Kochetkov
N K
NK
D000818:Animals; D002236:Carbohydrate Conformation; D002352:Carrier Proteins / Q000737:chemistry*; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D004529:Egg White; D006023:Glycoproteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D026901:Membrane Transport Proteins; D009844:Oligosaccharides / Q000737:chemistry*
D002352:Carrier Proteins; D006023:Glycoproteins; D026901:Membrane Transport Proteins; D009844:Oligosaccharides; C019079:riboflavin-binding protein
Struktura uglevodnykh tsepeĭ riboflavinsviazyvaiushchego glikoproteinabelka kurinogo iaĭtsa. Neĭtral'nye oligosakharidy gibrid tipa.