New platform for simple and rapid protein-based affinity reactions

Abstract 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...

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Autores principales:	Kei Kubota, Takuya Kubo, Tetsuya Tanigawa, Toyohiro Naito, Koji Otsuka
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a7505426d50b459395c7bf62aa29c32a
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spelling	oai:doaj.org-article:a7505426d50b459395c7bf62aa29c32a2021-12-02T12:30:19ZNew platform for simple and rapid protein-based affinity reactions10.1038/s41598-017-00264-y2045-2322https://doaj.org/article/a7505426d50b459395c7bf62aa29c32a2017-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-00264-yhttps://doaj.org/toc/2045-2322Abstract 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.Kei KubotaTakuya KuboTetsuya TanigawaToyohiro NaitoKoji OtsukaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kei Kubota Takuya Kubo Tetsuya Tanigawa Toyohiro Naito Koji Otsuka New platform for simple and rapid protein-based affinity reactions
description	Abstract 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.
format	article
author	Kei Kubota Takuya Kubo Tetsuya Tanigawa Toyohiro Naito Koji Otsuka
author_facet	Kei Kubota Takuya Kubo Tetsuya Tanigawa Toyohiro Naito Koji Otsuka
author_sort	Kei Kubota
title	New platform for simple and rapid protein-based affinity reactions
title_short	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_sort	new platform for simple and rapid protein-based affinity reactions
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/a7505426d50b459395c7bf62aa29c32a
work_keys_str_mv	AT keikubota newplatformforsimpleandrapidproteinbasedaffinityreactions AT takuyakubo newplatformforsimpleandrapidproteinbasedaffinityreactions AT tetsuyatanigawa newplatformforsimpleandrapidproteinbasedaffinityreactions AT toyohironaito newplatformforsimpleandrapidproteinbasedaffinityreactions AT kojiotsuka newplatformforsimpleandrapidproteinbasedaffinityreactions
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New platform for simple and rapid protein-based affinity reactions

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