Demonstration of a new glycopeptidase, from jack-bean meal, acting on aspartylglucosylamine linkages.
Biochem Biophys Res Commun
; 112(1): 155-60, 1983 Apr 15.
Article
em En
| MEDLINE
| ID: mdl-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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Base de dados:
MEDLINE
Assunto principal:
Plantas Medicinais
/
Acetilglucosamina
/
Amidoidrolases
/
Glucosamina
/
Fabaceae
Idioma:
En
Ano de publicação:
1983
Tipo de documento:
Article