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231224s2013 xx |||||o 00| ||eng c |
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|a 10.1021/la404051c
|2 doi
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|a pubmed24n0776.xml
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|a (DE-627)NLM233050809
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|a (NLM)24274382
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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 Pattammattel, Ajith
|e verfasserin
|4 aut
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| 245 |
1 |
0 |
|a Tuning the activities and structures of enzymes bound to graphene oxide with a protein glue
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|c 2013
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 15.04.2015
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|a Date Revised 16.11.2017
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Graphene oxide (GO) is being investigated extensively for enzyme and protein binding, but many enzymes bound to GO denature considerably and lose most of their activities. A simple, novel, and efficient approach is described here for improving the structures and activities of enzymes bound to GO such that bound enzymes are nearly as active as those of the corresponding unbound enzymes. Our strategy is to preadsorb highly cationized bovine serum albumin (cBSA) to passivate GO, and cBSA/GO (bGO) served as an excellent platform for enzyme binding. The binding of met-hemoglobin, glucose oxidase, horseradish peroxidase, BSA, catalase, lysozyme, and cytochrome c indicated improved binding, structure retention, and activities. Nearly 100% of native-like structures of all the seven proteins/enzymes were noted at near monolayer formation of cBSA on GO (400% w/w), and all bound enzymes indicated 100% retention of their activities. A facile, benign, simple, and general method has been developed for the biofunctionalization of GO, and this approach of coating with suitable protein glues expands the utility of GO as an advanced biophilic nanomaterial for applications in catalysis, sensing, and biomedicine
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|a Journal Article
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Adhesives
|2 NLM
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|a Enzymes, Immobilized
|2 NLM
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|a Oxides
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|a Serum Albumin, Bovine
|2 NLM
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|a 27432CM55Q
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|a Graphite
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|a 7782-42-5
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|a Cytochromes c
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|a 9007-43-6
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|a Glucose Oxidase
|2 NLM
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| 650 |
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|a EC 1.1.3.4
|2 NLM
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|a Horseradish Peroxidase
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| 650 |
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|a EC 1.11.1.-
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|a Catalase
|2 NLM
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|a EC 1.11.1.6
|2 NLM
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|a Muramidase
|2 NLM
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|a EC 3.2.1.17
|2 NLM
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| 700 |
1 |
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|a Puglia, Megan
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Chakraborty, Subhrakanti
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Deshapriya, Inoka K
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Dutta, Prabir K
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kumar, Challa V
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 29(2013), 50 vom: 17. Dez., Seite 15643-54
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:29
|g year:2013
|g number:50
|g day:17
|g month:12
|g pages:15643-54
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|u http://dx.doi.org/10.1021/la404051c
|3 Volltext
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|h 15643-54
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