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Catabolism of glycoprotein glycans: Characterization of a lysosomal endo‐N‐acetyl‐β‐d‐glucosaminidase specific for glycans with a terminal chitobiose residue

European Journal of Biochemistry, ISSN: 1432-1033, Vol: 159, Issue: 2, Page: 381-385
1986
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Article Description

An endo‐N‐acetyl‐β‐d‐glucosaminidase active towards oligosaccharides with a reducing terminal [bis(N‐acetylglucosamine)] residue has been characterized in rat liver. The primary structure of its reaction products was determined using high‐resolution H‐NMR spectroscopy. The enzyme is predominantly located in the lysosomal fraction, presents a maximum of activity at pH 3.5 and is completely inactive towards conjugated glycans, i.e. glycoproteins and glycopeptides as well as on glycoasparagines. These results support the existence of a new pathway for the degradation of glycoprotein glycans inside the lysosome. In particular, this enzymic activity may be the origin of oligosaccharides bearing a single terminal reducing N‐acetylglucosamine residue which are excreted in the urine of patients with various exoglycosidase deficiencies. Copyright © 1986, Wiley Blackwell. All rights reserved

Bibliographic Details

Thierry BAUSSANT; Gérard STRECKER; Jean‐Michel ‐M WIERUSZESKI; Jean MONTREUIL; Jean‐Claude ‐C MICHALSKI

Wiley

Biochemistry, Genetics and Molecular Biology

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