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Demonstration of peptide:N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations.

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Plummer, T H, Elder, J H, Alexander, S, Phelan, A W, Tarentino, A L·1984·Journal of Biological Chemistry

Abstract

Endo-beta-N-acetylglucosaminidase F preparations from Flavobacterium meningosepticum have been found to contain peptide:N-glycosidase activity. Only the second activity, designated as peptide:N-glycosidase F, readily cleaves the beta-aspartylglycosylamine linkage of a fetuin triantennary complex glycopeptide, as shown by the isolation of the corresponding carbohydrate-free peptide containing aspartic acid and of an intact oligosaccharide with a di-N-acetylchitobiosyl moiety at the reducing end. Both activities in the mixture will hydrolyze a high mannose octaglycopeptide from ovalbumin, with the type of product formed being influenced by pH. At pH 4.0, only the endo-beta-N-acetylglucosaminidase F activity is functional, releasing octapeptide-GlcNAc and oligosaccharide-GlcNAc. At pH 9.3, the predominant cleavage is by peptide:N-glycosidase F at the glycosylamine bond, releasing octapeptide and oligosaccharide-GlcNAc-GlcNAc. This latter oligosaccharide is then hydrolyzed by endo-beta-N-acetylglucosaminidase F to oligosaccharide-GlcNAc plus GlcNAc.

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Metadata

Authors
Plummer, T. H., Elder, J. H., Alexander, S., Phelan, A. W., & Tarentino, A. L.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1984-09
Volume
259
Issue
17
Pages
10700-10704
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1497028439
Cited by
587
References
0
FWCI
13.92
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Demonstration of peptide:N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations. https://app.cochat.ai/papers/10.1016/s0021-9258(18)90568-5
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Plummer, T. H., Elder, J. H., Alexander, S., Phelan, A. W., & Tarentino, A. L. (1984). Demonstration of peptide:N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)90568-5

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