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231224s2012 xx |||||o 00| ||eng c |
| 024 |
7 |
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|a 10.1021/la2043312
|2 doi
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|a pubmed24n0717.xml
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|a (DE-627)NLM215283198
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|a (NLM)22320263
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Kurinomaru, Takaaki
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Improved complementary polymer pair system
|b switching for enzyme activity by PEGylated polymers
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|c 2012
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 29.06.2012
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|a Date Revised 01.12.2018
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a The development of technology for on/off switching of enzyme activity is expected to expand the applications of enzyme in a wide range of research fields. We have previously developed a complementary polymer pair system (CPPS) that enables the activity of several enzymes to be controlled by a pair of oppositely charged polymers. However, it failed to control the activity of large and unstable α-amylase because the aggregation of the complex between anionic α-amylase and cationic poly(allylamine) (PAA) induced irreversible denaturation of the enzyme. To address this issue, we herein designed and synthesized a cationic copolymer with a poly(ethylene glycol) backbone, poly(N,N-diethylaminoethyl methacrylate)-block-poly(ethylene glycol) (PEAMA-b-PEG). In contrast to PAA, α-amylase and β-galactosidase were inactivated by PEAMA-b-PEG with the formation of soluble complexes. The enzyme/PEAMA-b-PEG complexes were then successfully recovered from the complex by the addition of anionic poly(acrylic acid) (PAAc). Thus, dispersion of the complex by PEG segment in PEAMA-b-PEG clearly plays a crucial role for regulating the activities of these enzymes, suggesting that PEGylated charged polymer is a new candidate for CPPS for large and unstable enzymes
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Polymers
|2 NLM
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|a Polyethylene Glycols
|2 NLM
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|a 3WJQ0SDW1A
|2 NLM
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|a alpha-Amylases
|2 NLM
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| 650 |
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|a EC 3.2.1.1
|2 NLM
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| 650 |
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|a beta-Galactosidase
|2 NLM
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| 650 |
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|a EC 3.2.1.23
|2 NLM
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| 700 |
1 |
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|a Tomita, Shunsuke
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kudo, Shinpei
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ganguli, Sumon
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Nagasaki, Yukio
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Shiraki, Kentaro
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 28(2012), 9 vom: 06. März, Seite 4334-8
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
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|g volume:28
|g year:2012
|g number:9
|g day:06
|g month:03
|g pages:4334-8
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|u http://dx.doi.org/10.1021/la2043312
|3 Volltext
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