title: Investigation by 360-MHz 1H-nuclear-magnetic-resonance spectroscopy and methylation analysis of the single glycan chain of chicken ovotransferrin.
abstract: 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.
mesh_terms: 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
chemical_list: D002241:Carbohydrates; D004527:Egg Proteins; D006020:Glycopeptides; D010446:Peptide Fragments; D003207:Conalbumin