Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.14/126560
34 Visitors
39 Hits
0 Downloads
- Title
- Mucin-type O-glycosylation – putting the pieces together
- Related
- The FEBS journal, Vol. 277, No. 1 (2010), p.81-94
- DOI
- 10.1111/j.1742-4658.2009.07429.x
- Publisher
- Wiley-Blackwell
- Date
- 2010
- FoR/RFCD Code(s)
-
110100 Medical Biochemistry and Metabolomics
060100 Biochemistry and Cell Biology
- Author/Creator
- Jensen, Pia H
- Author/Creator
- Kolarich, Daniel
- Author/Creator
- Packer, Nicolle H
- Description
- The O-glycosylation of Ser and Thr by N-acetylgalactosamine-linked (mucin-type) oligosaccharides is often overlooked in protein analysis. Three characteristics make O-linked glycosylation more difficult to analyse than N-linked glycosylation, namely: (a) no amino acid consensus sequence is known; (b) there is no universal enzyme for the release of O-glycans from the protein backbone; and (c) the density and number of occupied sites may be very high. For significant biological conclusions to be drawn, the complete picture of O-linked glycosylation on a protein needs to be determined. This review specifically addresses the analytical approaches that have been used, and the challenges remaining, in the characterization of both the composition and structure of mucin-type O-glycans, and the determination of the occupancy and heterogeneity at each amino acid attachment site.
- Description
- 14 page(s)
- Subject Keyword
- 110100 Medical Biochemistry and Metabolomics
- Subject Keyword
- 060100 Biochemistry and Cell Biology
- Subject Keyword
- electron transfer dissociation (ETD)/electron capture dissociation (ECD)
- Subject Keyword
- glycopeptides
- Subject Keyword
- MS
- Subject Keyword
- mucin oligosaccharides
- Subject Keyword
- O-glycosylation
- Subject Keyword
- released glycans
- Subject Keyword
- site specificity
- Resource Type
- journal article
- Organisation
- Macquarie University. Australian Proteome Analysis Facility (APAF)
- Organisation
- Macquarie University. Dept. of Chemistry and Biomolecular Sciences
- Identifier
- http://hdl.handle.net/1959.14/126560
- Identifier
- ISSN:1742-464X
- Identifier
- mq-rm-2010005189
- Language
- eng
- Reviewed
