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231223s2011 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2010.12.006
|2 doi
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|a pubmed24n1222.xml
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|a (DE-627)NLM205444024
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|a (NLM)21276727
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Duff, Stephen M G
|e verfasserin
|4 aut
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|a A kinetic comparison of asparagine synthetase isozymes from higher plants
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|c 2011
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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
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|2 rdacarrier
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|a Date Completed 17.10.2011
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|a Date Revised 13.12.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2011 Elsevier Masson SAS. All rights reserved.
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|a Four previously identified maize asparagine synthetase (AsnS) genes and a soy AsnS gene have been cloned and expressed in Escherichia coli. The enzymes have been purified and kinetically characterized. The plant AsnS proteins were expressed mainly in the inclusion bodies although small amounts of one form (ZmAsnS2) were recovered in the soluble fraction. In order to measure the kinetic properties of these enzymes a sensitive assay based on the detection of Asn by HPLC has been developed. In addition a method to refold the recombinant plant AsnS to produce active enzyme has been developed. The plant AsnS enzymes are kinetically distinct with substantial differences in K(m) (Gln) and V(max) values when compared to each other. These differences may be important factors for transgenic studies using AsnS genes for crop improvement
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|a Comparative Study
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|a Journal Article
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|a Isoenzymes
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Recombinant Proteins
|2 NLM
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|a Aspartate-Ammonia Ligase
|2 NLM
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|a EC 6.3.1.1
|2 NLM
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|a Qi, Qungang
|e verfasserin
|4 aut
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|a Reich, Timothy
|e verfasserin
|4 aut
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1 |
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|a Wu, Xiaoyun
|e verfasserin
|4 aut
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|a Brown, Todd
|e verfasserin
|4 aut
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|a Crowley, James H
|e verfasserin
|4 aut
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|a Fabbri, Brad
|e verfasserin
|4 aut
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 49(2011), 3 vom: 31. März, Seite 251-6
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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|g volume:49
|g year:2011
|g number:3
|g day:31
|g month:03
|g pages:251-6
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|u http://dx.doi.org/10.1016/j.plaphy.2010.12.006
|3 Volltext
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|d 49
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