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  • Investigation by 360-MHz 1H-nuclear-magnetic-resonance spectroscopy and methylation analysis of the single glycan chain of chicken ovotransferrin.

Investigation by 360-MHz 1H-nuclear-magnetic-resonance spectroscopy and methylation analysis of the single glycan chain of chicken ovotransferrin.

European journal of biochemistry (1979-10-15)
L Dorland, J Haverkamp, J F Vliegenthart, G Spik, B Fournet, J Montreuil
PMID574451
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.