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
- 34Citations
- 4Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations34
- Citation Indexes34
- 34
- CrossRef33
- Captures4
- Readers4
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
Wiley
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