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231223s2009 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2008.09.010
|2 doi
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|a pubmed24n0616.xml
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|a (DE-627)NLM184767679
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|a (NLM)19038476
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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 Chen, Xiong-Yan
|e verfasserin
|4 aut
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| 245 |
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|a Proteomics of weakly bound cell wall proteins in rice calli
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|c 2009
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 22.06.2009
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|a Date Revised 10.03.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a In the present work, we present a proteomic analysis of weakly bound cell wall proteins (CWPs) in rice. CWPs from rice calli were extracted with mannitol/CaCl(2), followed by back extraction with water-saturated phenol. The isolated CWPs were evaluated for contamination by cytosolic proteins by measuring the enzymatic activity of an intracellular marker (glucose-6-phosphate dehydrogenase). This revealed the presence of low levels of intracellular proteins and a significant enrichment of CWPs, as compared to the total extract. Protein samples were digested in gels with trypsin and analyzed using the multidimensional protein identification technology (MudPIT). A total of 292 proteins were identified, which included numerous classical CWPs and antioxidant proteins. Bioinformatics analysis showed that 72.6% of these proteins possessed a signal peptide, and a total of 198 proteins were determined to be CWPs in rice. Functional classification divided the extracellular proteins into different groups, including glycosyl hydrolases (23%), antioxidant proteins (12%), cell wall structure-related proteins (6%), metabolic pathways (9%), protein modifications (4%), defense (4%), and protease inhibitors (3%). Furthermore, comparative analysis of our identified rice CWPs with known Arabidopsis CWPs revealed 25 novel rice-specific CWPs. The study described here is an unprecedented large-scale analysis of CWPs in rice
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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| 650 |
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7 |
|a Plant Extracts
|2 NLM
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| 650 |
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|a Plant Proteins
|2 NLM
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| 650 |
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|a Protein Sorting Signals
|2 NLM
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| 650 |
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|a Glucosephosphate Dehydrogenase
|2 NLM
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| 650 |
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7 |
|a EC 1.1.1.49
|2 NLM
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| 700 |
1 |
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|a Kim, Sun Tae
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Cho, Won Kyong
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Rim, Yeonggil
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kim, Suwha
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kim, Seon-Won
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kang, Kyu Young
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Park, Zee Yong
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kim, Jae-Yean
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 166(2009), 7 vom: 01. Mai, Seite 675-85
|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:7
|g day:01
|g month:05
|g pages:675-85
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|u http://dx.doi.org/10.1016/j.jplph.2008.09.010
|3 Volltext
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|d 166
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|h 675-85
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