O-glycosylation in plant proteins

Čarija, Anita (2010) O-glycosylation in plant proteins. Bachelor's thesis, Faculty of Science > Department of Biology.

[img] PDF
Restricted to Registered users only
Language: Croatian

Download (750kB) | Request a copy

Abstract

Mucin-type O-glycosylation has been well characterized in mammalian systems but not in plants. The purified alcohol-soluble, non-reduced protein (prolamin) fraction from rice seed was investigated for the occurrence of O-linked oligosaccharides. As it is unlikely that storage prolamins are O-glycosylated, any O-gycosylation present in the extract could be attributable to co-extracted proteins, whether because of their association with the protein body or solubility. SDS-PAGE and MS analyses revealed 14 and 16 kDa protein families present in purified prolamin fractions that bound to the lectins peanut agglutinin (PNA), Vicia villosa lectin (VVL) and Jacalin, indicative of the presence of O-linked saccharides. A GlcNAc-containing O-linked carbohydrate moiety was discovered. Protein blotting with anti-O-GlcNAc antibody was positive in a subpopulation of the 14 kDa protein fraction, but a hot capping experiment was negative. Therefore, the GlcNAc residue is unlikely to be terminal. Fluorescent labeling and HPLC analysis demonstrated a peak consistent with Gal-β-(1→3)-GalNAc, with similar MS/MS fragmentation. O-glycosylation may contribute towards protein funcionality or regulation but further investigation is required to identify the specific proteins with these modifications.

Item Type: Thesis (Bachelor's thesis)
Supervisor: Balen, Biljana
Date: 2010
Number of Pages: 15
Subjects: NATURAL SCIENCES > Biology
Divisions: Faculty of Science > Department of Biology
Depositing User: Silvana Šehić
Date Deposited: 06 Oct 2014 09:12
Last Modified: 06 Oct 2014 09:12
URI: http://digre.pmf.unizg.hr/id/eprint/2926

Actions (login required)

View Item View Item

Nema podataka za dohvacanje citata