The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Control of glycoprotein synthesis.
Open accessAbstract
Hen oviduct membranes have been shown to catalyze the transfer of GlcNAc from UDP-GlcNAc to GlcNAc-beta 1-2Man alpha 1-6(GlcNAc beta 1-2 Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4GlcNAc-Asn-X (GnGn) to form the triantennary structure GlcNAc beta 1-2Man alpha 1-6[GlcNAc beta 1-2(GlcNAc beta 1-4)Man alpha 1-3]Man beta 1-4GlcNAc beta 1-4GlcNAc-Asn-X. The enzyme has been named UDP-GlcNAc:GnGn (GlcNAc to Man alpha 1-3) beta 4-N-acetylglucosaminyltransferase IV (GlcNAc-transferase IV) to distinguish it from three other hen oviduct GlcNAc-transferases designated I, II, and III. Since GlcNAc-transferases III and IV both act on the same substrate, concanavalin A/Sepharose was used to separate the products of the two enzymes. At pH 7.0 and at a Triton X-100 concentration of 0.125% (v/v), GlcNAc-transferase IV activity in hen oviduct membranes is 7 nmol/mg of protein/h. The product was characterized by high resolution proton NMR spectroscopy at 360 MHz and by methylation analysis. In addition to triantennary oligosaccharide, hen oviduct membranes produced about 20% of bisected triantennary material, GlcNAc beta 1-2Man alpha 1-6[GlcNAc beta 1-2(GlcNAc beta 1-4)Man alpha 1-3] [GlcNAc beta 1-4]Man beta 1-4GlcNAc beta 1-4GlcNAc-Asn-X. Maximal GlcNAc-transferase IV activity requires the presence of both terminal beta 1-2-linked GlcNAc residues in the substrate. Removal of the GlcNAc residue on the Man alpha 1-6 arm or of both GlcNAc residues reduces activity by at least 80%. A Gal beta 1-4GlcNAc disaccharide on the Man alpha 1-6 arm reduces activity by 68% while the presence of this disaccharide on the Man alpha 1-3 arm reduces activity to negligible levels. A similar substrate specificity was found for GlcNAc-transferase III, the enzyme which adds a bisecting GlcNAc in beta 1-4 linkage to the beta-linked Man residue. Since a bisecting GlcNAc was found to prevent GlcNAc-transferase IV action, the bisected triantennary material found in the incubation must have been formed by the sequential action of GlcNAc-transferase IV followed by GlcNAc-transferase III. Activities similar to GlcNAc-transferase IV were also detected in rat liver Golgi-rich membranes (0.4 nmol/mg/h) and pig thyroid microsomes (0.1 nmol/mg/h).
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Cites
Colorimetric Method for Determination of Sugars and Related Substances
DuBois, M., Gilles, K. A., Hamilton, J. K., Rebers, P. A., & Smith, F. (1956) · Analytical Chemistry · doi:10.1021/ac60111a017 · Cited by 52,269
Narasimhan, S., Stanley, P., & Schachter, H. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40339-5 · Cited by 159
Self-citation
Cited by
β1-6 Branching of Asn-Linked Oligosaccharides Is Directly Associated with Metastasis
Dennis, J. W., Laferté, S., Waghorne, C., Breitman, M. L., & Kerbel, R. S. (1987) · Science · doi:10.1126/science.2953071 · Cited by 940
Schachter, H. (1986) · Biochemistry and Cell Biology · doi:10.1139/o86-026 · Cited by 526
Self-citationSchachter, H. (1986) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4684-5209-9_2 · Cited by 508
Self-citationAdvances in the production of human therapeutic proteins in yeasts and filamentous fungi
Gerngross, T. U. (2004) · Nature Biotechnology · doi:10.1038/nbt1028 · Cited by 409
Taniguchi (2015) · doi:10.1016/bs.acr.2014.11.001 · Cited by 381
Metadata
- Authors
- Gleeson, P. A., & Schachter, H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1983-05
- Volume
- 258
- Issue
- 10
- Pages
- 6162-6173
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1482931197
- Cited by
- 240
- References
- 2
- FWCI
- 5.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
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