N-glycosylation potential of maize: the human lactoferrin used as a model
In order to determine the N-glycosylation potential of maize, a monocotyledon expression system for the production of recombinant glycoproteins, human lactoferrin was used as a model. The human lactoferrin coding sequence was inserted into the pUC18 plasmid under control of the wheat glutenin promot...
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| Veröffentlicht in: | Glycoconjugate journal 2001-07, Vol.18 (7), p.519 |
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| container_title | Glycoconjugate journal |
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| creator | Samyn-Petit, B Gruber, V Flahaut, C Wajda-Dubos, J P Farrer, S Pons, A Desmaizieres, G Slomianny, M C Theisen, M Delannoy, P |
| description | In order to determine the N-glycosylation potential of maize, a monocotyledon expression system for the production of recombinant glycoproteins, human lactoferrin was used as a model. The human lactoferrin coding sequence was inserted into the pUC18 plasmid under control of the wheat glutenin promoter. Maize was stably transformed and recombinant lactoferrin was purified from the fourth generation seeds. Glycosylation was analysed by gas chromatography, lectin detection, glycosidase digestions and mass spectrometry. The results indicated that both N-glycosylation sites of recombinant lactoferrin are mainly substituted by typical plant paucimannose-type glycans, with beta1,2-xylose and alpha1,3-linked fucose at the proximal N-acetylglucosamine, and that complex-type glycans with Lewis(a) determinants are not present in maize recombinant lactoferrin. |
| doi_str_mv | 10.1023/a:1019640312730 |
| format | Article |
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The human lactoferrin coding sequence was inserted into the pUC18 plasmid under control of the wheat glutenin promoter. Maize was stably transformed and recombinant lactoferrin was purified from the fourth generation seeds. Glycosylation was analysed by gas chromatography, lectin detection, glycosidase digestions and mass spectrometry. The results indicated that both N-glycosylation sites of recombinant lactoferrin are mainly substituted by typical plant paucimannose-type glycans, with beta1,2-xylose and alpha1,3-linked fucose at the proximal N-acetylglucosamine, and that complex-type glycans with Lewis(a) determinants are not present in maize recombinant lactoferrin.</description><identifier>ISSN: 0282-0080</identifier><identifier>EISSN: 1573-4986</identifier><identifier>DOI: 10.1023/a:1019640312730</identifier><identifier>PMID: 12151713</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>Blotting, Western ; Glycosylation ; Humans ; Lactoferrin - metabolism ; Mass spectrometry ; Medical research ; Models, Chemical ; Recombinant Proteins - metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Zea mays - metabolism</subject><ispartof>Glycoconjugate journal, 2001-07, Vol.18 (7), p.519</ispartof><rights>Kluwer Academic Publishers 2001</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c344t-cff40aa2699b6678f72dd633145e8b4a1a360d8c7cf5f616317bbe3bb2bfcd923</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,27931,27932</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12151713$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Samyn-Petit, B</creatorcontrib><creatorcontrib>Gruber, V</creatorcontrib><creatorcontrib>Flahaut, C</creatorcontrib><creatorcontrib>Wajda-Dubos, J P</creatorcontrib><creatorcontrib>Farrer, S</creatorcontrib><creatorcontrib>Pons, A</creatorcontrib><creatorcontrib>Desmaizieres, G</creatorcontrib><creatorcontrib>Slomianny, M C</creatorcontrib><creatorcontrib>Theisen, M</creatorcontrib><creatorcontrib>Delannoy, P</creatorcontrib><title>N-glycosylation potential of maize: the human lactoferrin used as a model</title><title>Glycoconjugate journal</title><addtitle>Glycoconj J</addtitle><description>In order to determine the N-glycosylation potential of maize, a monocotyledon expression system for the production of recombinant glycoproteins, human lactoferrin was used as a model. 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| subjects | Blotting, Western Glycosylation Humans Lactoferrin - metabolism Mass spectrometry Medical research Models, Chemical Recombinant Proteins - metabolism Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Zea mays - metabolism |
| title | N-glycosylation potential of maize: the human lactoferrin used as a model |
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