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Individual anomeric protons that are unresolved in the one-dimensional 250-MHz spectra of oligomannosidic glycopeptides can be separated and characterized by two-dimensional J-resolved NMR spectroscopy. Homogeneous preparations of ovalbumin glycopeptides Man6GlcNAc2Asn and Man5GlcNAc2Asn were characterized by chemical methods, conventional proton NMR, and two-dimensional J-resolved NMR. Due to characteristic differences in coupling constants, mannose (J1,2 less than or equal to 2 Hz) and N-acetylglucosamine (J1,2 approximately 9 Hz) anomeric signals of similar chemical shift were readily separated and identified in the two-dimensional spectra. It is shown that two-dimensional J-resolved NMR spectroscopy, in combination with conventional NMR and limited chemical analysis, is a rapid and reliable technique for the determination of glycopeptide primary structure.
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Bruch et al. (1982) studied this question.
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