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231223s2007 xx ||||| 00| ||eng c |
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|a pubmed24n0582.xml
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|a (DE-627)NLM17446469X
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|a (NLM)17944500
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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 Asuri, Prashanth
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes
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| 264 |
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|c 2007
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| 336 |
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 08.02.2008
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|a Date Revised 21.11.2013
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a We describe the structure, activity, and stability of enzymes covalently attached to single-walled carbon nanotubes (SWNTs). Conjugates of SWNTs with three functionally unrelated enzymes-horseradish peroxidase, subtilisin Carlsberg, and chicken egg white lysozyme-were found to be soluble in aqueous solutions. Furthermore, characterization of the secondary and tertiary structure of the immobilized proteins by circular dichroism and fluorescence spectroscopies, respectively, and determination of enzyme kinetics revealed that the enzymes retained a high fraction of their native structure and activity upon attachment to SWNTs. The SWNT-enzyme conjugates were also more stable in guanidine hydrochloride (GdnHCl) and at elevated temperatures relative to their solution counterparts. Thus, these protein conjugates represent novel preparations that possess the attributes of both soluble enzymes-high activity and low diffusional resistance-and immobilized enzymes-high stability-making them attractive choices for applications ranging from diagnostics and sensing to drug delivery
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|a Journal Article
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|a Research Support, N.I.H., Extramural
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|a Research Support, U.S. Gov't, Non-P.H.S.
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| 650 |
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|a Enzymes, Immobilized
|2 NLM
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|a Nanotubes, Carbon
|2 NLM
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|a Water
|2 NLM
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|a 059QF0KO0R
|2 NLM
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|a Horseradish Peroxidase
|2 NLM
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| 650 |
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|a EC 1.11.1.-
|2 NLM
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| 650 |
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|a Muramidase
|2 NLM
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| 650 |
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|a EC 3.2.1.17
|2 NLM
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| 650 |
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|a Subtilisins
|2 NLM
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| 650 |
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|a EC 3.4.21.-
|2 NLM
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| 650 |
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|a Guanidine
|2 NLM
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| 650 |
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|a JU58VJ6Y3B
|2 NLM
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| 700 |
1 |
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|a Bale, Shyam Sundhar
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Pangule, Ravindra C
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Shah, Dhiral A
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kane, Ravi S
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Dordick, Jonathan S
|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 23(2007), 24 vom: 20. Nov., Seite 12318-21
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
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|g volume:23
|g year:2007
|g number:24
|g day:20
|g month:11
|g pages:12318-21
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|a GBV_ILN_22
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|a GBV_ILN_350
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|a GBV_ILN_721
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|a AR
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|d 23
|j 2007
|e 24
|b 20
|c 11
|h 12318-21
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