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|a pubmed24n1221.xml
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|a (DE-627)NLM163535507
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|a (NLM)16777263
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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 Wang, Zhi-Qiang
|e verfasserin
|4 aut
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|a Glutamine synthetase and glutamate dehydrogenase contribute differentially to proline accumulation in leaves of wheat (Triticum aestivum) seedlings exposed to different salinity
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|c 2007
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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|a Date Completed 12.07.2007
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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 To investigate the roles of ammonium-assimilating enzymes in proline synthesis under salinity stress, the activities of glutamine synthetase (GS; EC 6.3.1.2) and NADH-dependent glutamate dehydrogenase (NADH-GDH; EC 1.4.1.2) were determined in leaves of wheat (Triticum aestivum) seedlings exposed to salt stress at 150 and 300 mM NaCl for 5d. At the lower salinity, only GS activity increased markedly. At 300 mM NaCl, however, NADH-GDH activity increased while GS activity decreased. A significant accumulation of proline was found only at high-salinity exposure while glutamate, a proline precursor, increased dramatically under both low and high salinity. These data suggests that GS-catalysis might be the main glutamate synthesis pathway under low salinity. At 300 mM NaCl, glutamate seems to be preferentially produced through the process catalyzed by NADH-GDH. The increase of ammonium in salinity-stressed wheat seedlings might have resulted from increased photorespiration, which is responsible for the higher NADH-GDH activity. The activity of Delta(1)-pyrroline-5-carboxylate reductase (P5CR; EC 1.5.1.2) was significantly enhanced at 300 mM NaCl but remained unchanged at 150 mM. Delta(1)-Pyrroline-5-carboxylate synthetase (P5CS) activity did not show a specific response, indicating that P5CR might be the limiting step in proline synthesis from glutamate at high salinity
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Amino Acids
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Quaternary Ammonium Compounds
|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 Sodium Chloride
|2 NLM
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|a 451W47IQ8X
|2 NLM
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|a Proline
|2 NLM
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|a 9DLQ4CIU6V
|2 NLM
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|a Isocitrate Dehydrogenase
|2 NLM
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|a EC 1.1.1.41
|2 NLM
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|a isocitrate dehydrogenase (NADP+)
|2 NLM
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|a EC 1.1.1.42
|2 NLM
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|a Glutamate Dehydrogenase
|2 NLM
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|a EC 1.4.1.2
|2 NLM
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|a Glutamate Dehydrogenase (NADP+)
|2 NLM
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|a EC 1.4.1.4
|2 NLM
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|a Pyrroline Carboxylate Reductases
|2 NLM
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|a EC 1.5.1.-
|2 NLM
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|a Glutamate-Ammonia Ligase
|2 NLM
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|a EC 6.3.1.2
|2 NLM
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|a Nitrogen
|2 NLM
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|a N762921K75
|2 NLM
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|a Yuan, Yong-Ze
|e verfasserin
|4 aut
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|a Ou, Ji-Quan
|e verfasserin
|4 aut
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|a Lin, Qing-Hua
|e verfasserin
|4 aut
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|a Zhang, Chu-Fu
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 164(2007), 6 vom: 14. Juni, Seite 695-701
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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1 |
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|g volume:164
|g year:2007
|g number:6
|g day:14
|g month:06
|g pages:695-701
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a GBV_NLM
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|a GBV_ILN_350
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|a AR
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|d 164
|j 2007
|e 6
|b 14
|c 06
|h 695-701
|