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231223s2009 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2009.01.014
|2 doi
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|a pubmed24n0626.xml
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|a (DE-627)NLM187642230
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|a (NLM)19346029
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|a (PII)S0176-1617(09)00096-0
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a García-Angulo, Penélope
|e verfasserin
|4 aut
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| 245 |
1 |
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|a High peroxidase activity and stable changes in the cell wall are related to dichlobenil tolerance
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|c 2009
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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 27.10.2009
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Suspension-cultured bean cells habituated to growth in a lethal concentration of dichlobenil were cultured for 3-5 years in a medium lacking the inhibitor in order to obtain long-term dehabituated cell lines. The growth parameters, cell morphology and ultrastructure of cells in the absence of dichlobenil reverted to that of non-habituated cells. The cellulose content and Fourier transform infrared (FTIR) spectra of crude cell walls from long-term dehabituated cells were also similar to those of non-habituated cells. However, long-term dehabituated cells showed three times more tolerance to dichlobenil than non-habituated cells. The incorporation of [(14)C]Glc into cellulose was reduced by 40% in dehabituated cells when compared with non-habituated cells. However, the addition of dichlobenil to dehabituated cells increased the incorporation of [(14)C]Glc into cellulose 3.3-fold with respect to that of non-habituated cells. Dehabituated cells showed a constitutively increased peroxidase activity when compared with non-habituated cells. Results reported here indicate that the habituation of bean cultured cells to dichlobenil relied partially on a stable change in the cellulose biosynthesis complex and is associated with high guaiacol peroxidase activity
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Antioxidants
|2 NLM
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|a Nitriles
|2 NLM
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| 650 |
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|a Cellulose
|2 NLM
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|a 9004-34-6
|2 NLM
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|a Peroxidases
|2 NLM
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|a EC 1.11.1.-
|2 NLM
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|a Ascorbate Peroxidases
|2 NLM
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| 650 |
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|a EC 1.11.1.11
|2 NLM
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| 650 |
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|a Glutathione Peroxidase
|2 NLM
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| 650 |
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|a EC 1.11.1.9
|2 NLM
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| 650 |
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|a Glucose
|2 NLM
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| 650 |
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|a IY9XDZ35W2
|2 NLM
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| 650 |
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|a dichlobanil
|2 NLM
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| 650 |
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|a N42NR4196R
|2 NLM
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| 700 |
1 |
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|a Alonso-Simón, Ana
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Mélida, Hugo
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Encina, Antonio
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Acebes, José L
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Álvarez, Jesús M
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 166(2009), 12 vom: 15. Aug., Seite 1229-1240
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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| 773 |
1 |
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|g volume:166
|g year:2009
|g number:12
|g day:15
|g month:08
|g pages:1229-1240
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| 856 |
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|u http://dx.doi.org/10.1016/j.jplph.2009.01.014
|3 Volltext
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|d 166
|j 2009
|e 12
|b 15
|c 08
|h 1229-1240
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