Investigation by 360-MHz 1H-Nuclear-Magnetic-Resonance Spectroscopy and Methylation Analysis of the Single Glycan Chain of Chicken Ovotransferrin
Open Access
- 1 October 1979
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 100 (2) , 569-574
- https://doi.org/10.1111/j.1432-1033.1979.tb04203.x
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: 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.This publication has 23 references indexed in Scilit:
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