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...
Main Authors: | , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2017-03-01
|
Series: | Scientific Reports |
Online Access: | https://doi.org/10.1038/s41598-017-00264-y |
id |
doaj-a7505426d50b459395c7bf62aa29c32a |
---|---|
record_format |
Article |
spelling |
doaj-a7505426d50b459395c7bf62aa29c32a2020-12-08T00:50:17ZengNature Publishing GroupScientific Reports2045-23222017-03-01711910.1038/s41598-017-00264-yNew platform for simple and rapid protein-based affinity reactionsKei Kubota0Takuya Kubo1Tetsuya Tanigawa2Toyohiro Naito3Koji Otsuka4Graduate School of Engineering, Kyoto UniversityGraduate School of Engineering, Kyoto UniversityGraduate School of Engineering, Kyoto UniversityGraduate School of Engineering, Kyoto UniversityGraduate School of Engineering, Kyoto UniversityAbstract 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.https://doi.org/10.1038/s41598-017-00264-y |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Kei Kubota Takuya Kubo Tetsuya Tanigawa Toyohiro Naito Koji Otsuka |
spellingShingle |
Kei Kubota Takuya Kubo Tetsuya Tanigawa Toyohiro Naito Koji Otsuka New platform for simple and rapid protein-based affinity reactions Scientific Reports |
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 Publishing Group |
series |
Scientific Reports |
issn |
2045-2322 |
publishDate |
2017-03-01 |
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. |
url |
https://doi.org/10.1038/s41598-017-00264-y |
work_keys_str_mv |
AT keikubota newplatformforsimpleandrapidproteinbasedaffinityreactions AT takuyakubo newplatformforsimpleandrapidproteinbasedaffinityreactions AT tetsuyatanigawa newplatformforsimpleandrapidproteinbasedaffinityreactions AT toyohironaito newplatformforsimpleandrapidproteinbasedaffinityreactions AT kojiotsuka newplatformforsimpleandrapidproteinbasedaffinityreactions |
_version_ |
1724395810472329216 |