[Isolation and characteristics of carbohydrate chains of riboflavin-binding glycoprotein from the chicken egg].
Isolation and characterization of oligosaccharides of riboflavin binding glycoprotein from hen white is described. Reductive cleavage of the N-glycosylamide carbohydrate-peptide bond with LiBH4/tert-BuOH followed by NaBH4-NaOH treatment gave rise to alditols, which were fractionated by means of HPLC. Twelve alditols were isolated in quantities sufficient for the monosaccharide analysis. Possibility of an ovomucoid-type oligosaccharide structure for all the alditols is discussed.
D000818:Animals; D002352:Carrier Proteins / Q000032:analysis*; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D004527:Egg Proteins / Q000032:analysis*; D006020:Glycopeptides / Q000032:analysis / Q000302:isolation & purification*; D026901:Membrane Transport Proteins; D009844:Oligosaccharides / Q000032:analysis / Q000302:isolation & purification*
D002352:Carrier Proteins; D004527:Egg Proteins; D006020:Glycopeptides; D026901:Membrane Transport Proteins; D009844:Oligosaccharides; C019079:riboflavin-binding protein
Vydelenie i kharakteristika uglevodnykh tsepeĭ riboflavinsviazyvaiushchego glikoproteina belka kurinogo iaĭtsa.