Reversible protein affinity-labelling using bromomaleimide-based reagents

Reversible protein biotinylation is readily affected via conjugation with a bromomaleimide-based reagent followed by reductive cleavage. The intermediate biotinylated protein constructs are stable at physiological temperature and pH 8.0. Quantitative reversibility is elegantly delivered under mild c...

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Detalles Bibliográficos
Autores principales: Nathani, Ramiz I., Chudasama, Vijay, Ryan, Chris P., Moody, Paul R., Morgan, Rachel E., Fitzmaurice, Richard J., Smith, Mark E. B., Baker, James R., Caddick, Stephen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2013
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3763775/
https://www.ncbi.nlm.nih.gov/pubmed/23462873
http://dx.doi.org/10.1039/c3ob40239h
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author Nathani, Ramiz I.
Chudasama, Vijay
Ryan, Chris P.
Moody, Paul R.
Morgan, Rachel E.
Fitzmaurice, Richard J.
Smith, Mark E. B.
Baker, James R.
Caddick, Stephen
author_facet Nathani, Ramiz I.
Chudasama, Vijay
Ryan, Chris P.
Moody, Paul R.
Morgan, Rachel E.
Fitzmaurice, Richard J.
Smith, Mark E. B.
Baker, James R.
Caddick, Stephen
author_sort Nathani, Ramiz I.
collection PubMed
description Reversible protein biotinylation is readily affected via conjugation with a bromomaleimide-based reagent followed by reductive cleavage. The intermediate biotinylated protein constructs are stable at physiological temperature and pH 8.0. Quantitative reversibility is elegantly delivered under mild conditions of using a stoichiometric amount of a bis-thiol, thus providing an approach that will be of general interest in chemical biology and proteomics.
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spelling pubmed-37637752013-09-05 Reversible protein affinity-labelling using bromomaleimide-based reagents Nathani, Ramiz I. Chudasama, Vijay Ryan, Chris P. Moody, Paul R. Morgan, Rachel E. Fitzmaurice, Richard J. Smith, Mark E. B. Baker, James R. Caddick, Stephen Org Biomol Chem Chemistry Reversible protein biotinylation is readily affected via conjugation with a bromomaleimide-based reagent followed by reductive cleavage. The intermediate biotinylated protein constructs are stable at physiological temperature and pH 8.0. Quantitative reversibility is elegantly delivered under mild conditions of using a stoichiometric amount of a bis-thiol, thus providing an approach that will be of general interest in chemical biology and proteomics. Royal Society of Chemistry 2013-03-21 2013-03-05 /pmc/articles/PMC3763775/ /pubmed/23462873 http://dx.doi.org/10.1039/c3ob40239h Text en This journal is © The Royal Society of Chemistry 2013 http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution 3.0 Unported License (http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Chemistry
Nathani, Ramiz I.
Chudasama, Vijay
Ryan, Chris P.
Moody, Paul R.
Morgan, Rachel E.
Fitzmaurice, Richard J.
Smith, Mark E. B.
Baker, James R.
Caddick, Stephen
Reversible protein affinity-labelling using bromomaleimide-based reagents
title Reversible protein affinity-labelling using bromomaleimide-based reagents
title_full Reversible protein affinity-labelling using bromomaleimide-based reagents
title_fullStr Reversible protein affinity-labelling using bromomaleimide-based reagents
title_full_unstemmed Reversible protein affinity-labelling using bromomaleimide-based reagents
title_short Reversible protein affinity-labelling using bromomaleimide-based reagents
title_sort reversible protein affinity-labelling using bromomaleimide-based reagents
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3763775/
https://www.ncbi.nlm.nih.gov/pubmed/23462873
http://dx.doi.org/10.1039/c3ob40239h
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