| Téléchargement | - Voir le manuscrit accepté : Cystine-mediated oligomerization of the Atlantic salmon serum C-type lectin (PDF, 792 Kio)
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| DOI | Trouver le DOI : https://doi.org/10.1016/j.bbapap.2010.11.004 |
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| Auteur | Rechercher : Hudson, David M.; Rechercher : Mattatall, Neil R.1; Rechercher : Uribe, Elke; Rechercher : Richards, Robert C.1; Rechercher : Gong, Huansheng1; Rechercher : Ewart, K. Vanya1 |
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| Affiliation | - Conseil national de recherches du Canada. Institut des biosciences marines du CNRC
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| Format | Texte, Article |
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| Sujet | Atlantic salmon; C-type lectin; Oligomerization; Disulfide bond; biotechnology; Biotechnology; Cell Adhesion; Cells; Comparative Study; crystal structure; Dimerization; EGF; Epidermal Growth Factor; Igg; Mesenchymal Stem Cells; Microarray; Microarrays; monitoring; NPArC; Phosphorylation; Polymers; Protein; Proteins; Recombinant protein; Recombinant Proteins; serum; Substrates; Tags; Tissue Engineering; Tyrosine |
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| Résumé | The Atlantic salmon (Salmo salar) serum lectin (SSL) is a C-type lectin that binds to bacteria including salmon pathogens. SSL has been shown to be oligomeric in salmon serum and it displays a stoichiometric band-laddering pattern when analyzed by SDS-PAGE under non-reducing conditions. In this study, a model was generated for SSL isoform 2 in silico in order to identify cysteines that are available to form intermolecular disulfide bonds facilitating oligomerization. Then, recombinant SSL was expressed in E. coli and mutants were produced at positions Cys72 and Cys149. The SSL preparations were purified by metal-affinity chromatography and shown to be functional by carbohydrate- affinity chromatography. The recombinant SSL formed oligomers, which were evident by non-reducing covalent cross-linking and non-reducing SDS-PAGE; however, the band patterns were different for the mutants, with the maximal and predominant multimer sizes distinct from the wild-type recombinant lectin. Further examination of oligomerization by size exclusion chromatography revealed a subunit number from 35 to at least 110 for the wild-type recombinant SSL and subunit numbers below 9 for each mutant SSL oligomer. Thus, both cysteines were found to contribute to oligomerization of SSL. © 2010 Published by Elsevier B.V. All rights reserved. |
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| Date de publication | 2011-02-01 |
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| Dans | |
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| Langue | anglais |
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| Publications évaluées par des pairs | Oui |
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| Numéro du CNRC | NRCC 51771 |
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| Numéro NPARC | 16616686 |
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| Exporter la notice | Exporter en format RIS |
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| Signaler une correction | Signaler une correction (s'ouvre dans un nouvel onglet) |
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| Identificateur de l’enregistrement | 2bd4ee6d-db04-48da-baac-e678f105495b |
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| Enregistrement créé | 2011-03-31 |
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| Enregistrement modifié | 2020-04-21 |
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