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231224s2011 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2011.02.007
|2 doi
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|a pubmed24n0691.xml
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|a (DE-627)NLM207364427
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|a (NLM)21481489
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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 Damaraju, Sridevi
|e verfasserin
|4 aut
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|a Functions of the water soluble chlorophyll-binding protein in 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
|b cr
|2 rdacarrier
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|a Date Completed 07.10.2011
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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 Copyright © 2011 Elsevier GmbH. All rights reserved.
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|a Functional aspects of water soluble chlorophyll-binding protein (WSCP) in plants were investigated during the courses of leaf senescence, chlorophyll biogenesis, stress response and photoprotection. The cDNA sequence encoding WSCP from cauliflower was cloned into a binary vector to facilitate Agrobacterium tumefaciens mediated transformation of Nicotiana tabacum. The resultant transgenic tobacco plants overexpressed the CauWSCP gene under the control of a 35S-promoter. Analyses of protein and pigment contents indicate that WSCP overexpression does not enhance chlorophyll catabolism in vivo, thus rendering a role of WSCP in Chl degradation unlikely. Accumulation of higher levels of protochlorophyllide in WSCP overexpressor plants corroborates a proposed temporary storage and carrier function of WSCP for chlorophyll and late precursors. Although WSCP overexpressor plants did not show significant differences in non-photochemical quenching of chlorophyll fluorescence, they are characterized by significantly lower zeaxanthin accumulation and peroxidase activity at different light intensities, even at high light intensities of 700-900μmol photons m(-2)s(-1). These results suggest a photoprotective function of the functional chlorophyll binding-WSCP tetramer by shielding of chlorophylls from molecular oxygen
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Light-Harvesting Protein Complexes
|2 NLM
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|a Peroxides
|2 NLM
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|a Plant Extracts
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Reactive Oxygen Species
|2 NLM
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|a Xanthophylls
|2 NLM
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|a Water
|2 NLM
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|a 059QF0KO0R
|2 NLM
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|a Chlorophyll
|2 NLM
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|a 1406-65-1
|2 NLM
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|a Peroxidase
|2 NLM
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|a EC 1.11.1.7
|2 NLM
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|a Oxidoreductases Acting on CH-CH Group Donors
|2 NLM
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|a EC 1.3.-
|2 NLM
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|a protochlorophyllide reductase
|2 NLM
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|a EC 1.3.1.33
|2 NLM
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| 700 |
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|a Schlede, Stephanie
|e verfasserin
|4 aut
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| 700 |
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|a Eckhardt, Ulrich
|e verfasserin
|4 aut
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| 700 |
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|a Lokstein, Heiko
|e verfasserin
|4 aut
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| 700 |
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|a Grimm, Bernhard
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 168(2011), 12 vom: 15. Aug., Seite 1444-51
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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| 773 |
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|g volume:168
|g year:2011
|g number:12
|g day:15
|g month:08
|g pages:1444-51
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|u http://dx.doi.org/10.1016/j.jplph.2011.02.007
|3 Volltext
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|d 168
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