Investigation by 360-MHz 1H-nuclear-magnetic-resonance spectroscopy and methylation analysis of the single glycan chain of chicken ovotransferrin.
The primary structure of two glycopeptides obtained by pronase digestion of chicken ovotransferrin has been investigated by 360-MHz proton nuclear magnetic resonance (NMR) spectroscopy and methylation analysis. The two glycopeptides differ in amino acid composition but contain the same carbohydrate moiety, viz: (formula: see text). Using the NMR data of some reference compounds the chemical shifts of the anomeric protons and mannose H-2 protons could be predicted with an accuracy of 0.01 ppm.
D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002241:Carbohydrates / Q000032:analysis; D002645:Chickens; D003207:Conalbumin; D004527:Egg Proteins; D004529:Egg White; D006020:Glycopeptides; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments / Q000032:analysis
D002241:Carbohydrates; D004527:Egg Proteins; D006020:Glycopeptides; D010446:Peptide Fragments; D003207:Conalbumin