New platform for simple and rapid protein-based affinity reactions

Kei Kubota; Takuya Kubo; Tetsuya Tanigawa; Toyohiro Naito; Koji Otsuka

doi:10.1038/s41598-017-00264-y

New platform for simple and rapid protein-based affinity reactions

Kei Kubota, Takuya Kubo, Tetsuya Tanigawa, Toyohiro Naito, Koji Otsuka

研究成果: Contribution to journal › Article › 査読

8 被引用数 (Scopus)

抄録

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.

本文言語	英語
論文番号	178
ジャーナル	Scientific reports
巻	7
号	1
DOI	https://doi.org/10.1038/s41598-017-00264-y
出版ステータス	出版済み - 2017
外部発表	はい

All Science Journal Classification (ASJC) codes

General

文献へのアクセス

10.1038/s41598-017-00264-y

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引用スタイル

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note = "Funding Information: This research was partly supported by the Grant-in Aid for Scientific Research (15K13756) from the Japan Society for the Promotion of Science, Shimadzu Science Foundation, and Kurita Water and Environment Foundation. Publisher Copyright: {\textcopyright} The Author(s) 2017.",

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AU - Kubo, Takuya

AU - Tanigawa, Tetsuya

AU - Naito, Toyohiro

AU - Otsuka, Koji

N1 - Funding Information: This research was partly supported by the Grant-in Aid for Scientific Research (15K13756) from the Japan Society for the Promotion of Science, Shimadzu Science Foundation, and Kurita Water and Environment Foundation. Publisher Copyright: © The Author(s) 2017.

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N2 - 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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