New platform for simple and rapid protein-based affinity reactions

We developed a spongy-like porous polymer (spongy monolith) consisting of poly(ethylene-co-glycidyl methacrylate) with continuous macropores that allowed efficient in situ reaction between the epoxy groups and proteins of interest. Immobilization of protein A on the spongy monolith enabled high-yiel...

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Autores principales: Kubota, Kei, Kubo, Takuya, Tanigawa, Tetsuya, Naito, Toyohiro, Otsuka, Koji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5428043/
https://www.ncbi.nlm.nih.gov/pubmed/28282970
http://dx.doi.org/10.1038/s41598-017-00264-y
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author Kubota, Kei
Kubo, Takuya
Tanigawa, Tetsuya
Naito, Toyohiro
Otsuka, Koji
author_facet Kubota, Kei
Kubo, Takuya
Tanigawa, Tetsuya
Naito, Toyohiro
Otsuka, Koji
author_sort Kubota, Kei
collection PubMed
description We developed a spongy-like porous polymer (spongy monolith) consisting of poly(ethylene-co-glycidyl methacrylate) with continuous macropores that allowed efficient in situ reaction between the epoxy groups and proteins of interest. Immobilization of protein A on the spongy monolith enabled high-yield collection of immunoglobulin G (IgG) from cell culture supernatant even at a high flow rate. In addition, immobilization of pepsin on the spongy monolith enabled efficient online digestion at a high flow rate.
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spelling pubmed-54280432017-05-15 New platform for simple and rapid protein-based affinity reactions Kubota, Kei Kubo, Takuya Tanigawa, Tetsuya Naito, Toyohiro Otsuka, Koji Sci Rep Article We developed a spongy-like porous polymer (spongy monolith) consisting of poly(ethylene-co-glycidyl methacrylate) with continuous macropores that allowed efficient in situ reaction between the epoxy groups and proteins of interest. Immobilization of protein A on the spongy monolith enabled high-yield collection of immunoglobulin G (IgG) from cell culture supernatant even at a high flow rate. In addition, immobilization of pepsin on the spongy monolith enabled efficient online digestion at a high flow rate. Nature Publishing Group UK 2017-03-14 /pmc/articles/PMC5428043/ /pubmed/28282970 http://dx.doi.org/10.1038/s41598-017-00264-y Text en © The Author(s) 2017 This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Kubota, Kei
Kubo, Takuya
Tanigawa, Tetsuya
Naito, Toyohiro
Otsuka, Koji
New platform for simple and rapid protein-based affinity reactions
title New platform for simple and rapid protein-based affinity reactions
title_full New platform for simple and rapid protein-based affinity reactions
title_fullStr New platform for simple and rapid protein-based affinity reactions
title_full_unstemmed New platform for simple and rapid protein-based affinity reactions
title_short New platform for simple and rapid protein-based affinity reactions
title_sort new platform for simple and rapid protein-based affinity reactions
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5428043/
https://www.ncbi.nlm.nih.gov/pubmed/28282970
http://dx.doi.org/10.1038/s41598-017-00264-y
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