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231223s2008 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2007.12.002
|2 doi
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|a pubmed24n0591.xml
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|a (DE-627)NLM177311452
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|a (NLM)18242768
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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 Zhou, Rui
|e verfasserin
|4 aut
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|a Competitive inhibition of phosphoglucose isomerase of apple leaves by sorbitol 6-phosphate
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|c 2008
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 22.04.2009
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|a Date Revised 07.12.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Apple leaf cytosolic phosphoglucose isomerase (PGI, EC 5.3.1.9) was purified to an apparent homogeneity with a specific activity of 2456 units/mg protein, and chloroplastic PGI was partially purified to a specific activity of 72 units/mg protein to characterize their biochemical properties. These two isoforms showed differential responses to heat treatment; incubation at 50 degrees C for 10 min resulted in a complete loss of the chloroplastic PGI activity, whereas the cytosolic PGI only lost 50% of its activity. Apple cytosolic PGI is a dimeric enzyme with a molecular mass of 66 kDa for each monomer. The activity of both isoforms was strongly inhibited by erythrose 4-phosphate (E4P) with a K(i) of 1.2 and 3.0 microM for the cytosolic PGI and chloroplastic PGI, respectively. Sorbitol 6-phosphate (Sor6P), an intermediate in sorbitol biosynthesis, was found to be a competitive inhibitor for both cytosolic and chloroplastic PGIs with a K(i) of 61 and 40 microM, respectively. PGIs from both spinach and tomato leaves were also inhibited by Sor6P in a similar manner. The possible physiological significance of this finding is discussed
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|a Journal Article
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|a Fructosephosphates
|2 NLM
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|a Hexosephosphates
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|a Sugar Phosphates
|2 NLM
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|a sorbitol 6-phosphate
|2 NLM
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|a 20479-58-7
|2 NLM
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|a Glucose-6-Phosphate
|2 NLM
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|a 56-73-5
|2 NLM
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|a erythrose 4-phosphate
|2 NLM
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|a 585-18-2
|2 NLM
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|a fructose-6-phosphate
|2 NLM
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|a 6814-87-5
|2 NLM
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|a Carbohydrate Dehydrogenases
|2 NLM
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|a EC 1.1.-
|2 NLM
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|a Glucose-6-Phosphate Isomerase
|2 NLM
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|a EC 5.3.1.9
|2 NLM
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|a Cheng, Lailiang
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 165(2008), 9 vom: 16. Juni, Seite 903-10
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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|g volume:165
|g year:2008
|g number:9
|g day:16
|g month:06
|g pages:903-10
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|u http://dx.doi.org/10.1016/j.jplph.2007.12.002
|3 Volltext
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