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  • Title: Demonstration of a new glycopeptidase, from jack-bean meal, acting on aspartylglucosylamine linkages.
    Author: Sugiyama K, Ishihara H, Tejima S, Takahashi N.
    Journal: Biochem Biophys Res Commun; 1983 Apr 15; 112(1):155-60. PubMed ID: 6838602.
    Abstract:
    An enzyme preparation from jack-bean meal hydrolyzed beta-aspartylglucosylamine linkages in glycopeptides. The enzyme could release sialic acid-containing complex-type oligosaccharides as well as high-mannose-type and hybrid-type oligosaccharides. The products were equimolar amounts of ammonia, oligosaccharide and peptide. The enzyme cleaved glycopeptides with three or more amino acid residues, whereas it did not hydrolyze GlcNAc-Asn. The mechanism of action of the enzyme and substrate specificity so far tested were similar to those of the glycopeptidase from almonds.
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