Either high-mannose-type or hybrid-type oligosaccharide is linked to the same asparagine residue in ovalbumin
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference20 articles.
1. Structural studies of two ovalbumin glycopeptides in relation to the endo-beta-N-acetylglucosaminidase specificity.
2. Structures of the carbohydrate moiety of ovalbumin glycopeptide III and the difference in specificity of endo-beta-N-acetylglucosaminidases CII and H.
3. The structures of the galactose-containing sugar chains of ovalbumin.
4. Demonstration of a new amidase acting on glycopeptides
5. Complete structure of the carbohydrate moiety of stem bromelain. An application of the almond glycopeptidase for structural studies of glycopeptides.
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