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FEBS Lett ; 552(2-3): 170-6, 2003 Sep 25.
Article in English | MEDLINE | ID: mdl-14527682

ABSTRACT

Tobacco-based transient expression was employed to elucidate the impact of differential targeting to subcellular compartments on activity and quality of gastric lipase as a model for the production of recombinant glycoproteins in plants. Overall N-linked glycan structures of recombinant lipase were analyzed and for the first time sugar structures of its four individual N-glycosylation sites were determined in situ by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) on a trypsin digest without isolation or deglycosylation of the peptides. Three glycosylation sites contain both complex-type N-glycans and high-mannose-type structures, the fourth is exclusively linked to high-mannose glycans. Although the overall pattern of glycan structures is influenced by the targeting, our results show that the type of glycans found linked to a given Asn residue is largely influenced by the physico-chemical environment of the site. The transient tobacco system combined with MALDI-TOF-MS appears to be a useful tool for the evaluation of glycoprotein production in plants.


Subject(s)
Nicotiana/genetics , Recombinant Proteins/biosynthesis , Recombinant Proteins/genetics , Animals , Binding Sites , Carbohydrate Sequence , Dogs , Gene Expression , Glycoproteins/biosynthesis , Glycoproteins/chemistry , Glycoproteins/genetics , Glycosylation , In Vitro Techniques , Lipase/biosynthesis , Lipase/chemistry , Lipase/genetics , Molecular Sequence Data , Molecular Structure , Plants, Genetically Modified , Polysaccharides/chemistry , Recombinant Proteins/chemistry , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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