Analysis of Recombinant Protein S-Nitrosylation Using the Biotin-Switch Technique
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Titre | Analysis of Recombinant Protein S-Nitrosylation Using the Biotin-Switch Technique |
Type de publication | Book Chapter |
Year of Publication | 2018 |
Auteurs | Aime SEB, Hichami S, Wendehenne D, Lamotte O |
Editor | Mengel A, Lindermayr C |
Book Title | NITRIC OXIDE: Methods and Protocols |
Series Title | Methods in Molecular Biology |
Volume | 1747 |
Pagination | 131-141 |
Publisher | HUMANA PRESS INC |
City | 999 RIVERVIEW DR, STE 208, TOTOWA, NJ 07512-1165 USA |
ISBN Number | 978-1-4939-7695-9; 978-1-4939-7694-2 |
ISBN | 1064-3745 |
Mots-clés | Biotin switch, Nitric oxide, Recombinant protein, Redox-based posttranslational modification, S-nitrosation, S-nitrosothiols, S-nitrosylation |
Résumé | Nitric oxide is regarded as a key signaling messenger in several organisms. Its physiological relevance is partly due to its capacity to induce posttranslational modifications of proteins through its direct or indirect reaction with specific amino acid residues. Among them, S-nitrosylation has been shown to be involved in a broad range of cellular signaling pathways both in animals and plants. The identification of S-nitrosylated proteins has been made possible by the development of the Biotin-Switch Technique (BST) in the early 2000s. Here, we describe the BST protocol we routinely use to check in vitro S-nitrosylation of recombinant proteins induced by NO donors. |
DOI | 10.1007/978-1-4939-7695-9_11 |