Regulation of NADP-malate dehydrogenase in C4 plants: Effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems
Identifieur interne : 00DF88 ( Main/Curation ); précédent : 00DF87; suivant : 00DF89Regulation of NADP-malate dehydrogenase in C4 plants: Effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems
Auteurs : F. Rebeille [France] ; M. D. Hatch [Australie]Source :
- Archives of Biochemistry and Biophysics [ 0003-9861 ] ; 1986.
Descripteurs français
- Wicri :
- topic : Maïs.
English descriptors
- KwdEn :
- Assay, Biochem, Biophys, Chloroplast, Dehydrogenase, Dhap, Edta, Electron flux, Enzyme activity, Ferredoxin, Final concentration, Final concentrations, High ratios, Inactivation, Initial rate, Intact chloroplasts, Light intensity, Maize, Mesophyll, Mesophyll chloroplasts, Nadp, Nadp ratio, Nadp ratios, Nadph, Nadph concentration, Nadpmdh, Oxidized, Oxidized thioredoxin, Photosynthesis, Photosynthetic metabolites, Present studies, Pyridine nucleotide, Redox, Redox state, Reduceable, Reduceable substrates, Thiol groups, Thioredoxin, Thioredoxin content, Thioredoxin redox state, Total amount.
- Teeft :
- Assay, Biochem, Biophys, Chloroplast, Dehydrogenase, Dhap, Edta, Electron flux, Enzyme activity, Ferredoxin, Final concentration, Final concentrations, High ratios, Inactivation, Initial rate, Intact chloroplasts, Light intensity, Maize, Mesophyll, Mesophyll chloroplasts, Nadp, Nadp ratio, Nadp ratios, Nadph, Nadph concentration, Nadpmdh, Oxidized, Oxidized thioredoxin, Photosynthesis, Photosynthetic metabolites, Present studies, Pyridine nucleotide, Redox, Redox state, Reduceable, Reduceable substrates, Thiol groups, Thioredoxin, Thioredoxin content, Thioredoxin redox state, Total amount.
Abstract
Abstract: Activation and inactivation of NADP-malate dehydrogenase purified from Zea mays leaves were followed in a reconstituted system provided with thioredoxin poised in various redox states with dithiothreitol. The initial rate of activation or inactivation of NADP-malate dehydrogenase was proportional to the concentration of reduced or oxidized thioredoxin, respectively. The rate of inactivation was about 16 times that for activation at pH 7.4. Both activities increased when the pH was increased from 7.4 to 8.0. The redox potentials (E′0, pH 7) for the dithiol-disulfide systems of thioredoxin and NADP-malate dehydrogenase were estimated to be about −0.30 and −0.33 V, respectively. As would be predicted from these values, high proportions of active malate dehydrogenase were developed only in the presence of very high ratios of reduced to oxidized thioredoxin. Similarly, when pyridine nucleotide was included, a high degree of activation of malate dehydrogenase was only observed with high NADPHNADP ratios. These results confirm predictions based on models developed in earlier studies that the NADPH to NADP ratio as well as the thioredoxin redox state may be critical in determining the level of NADP-malate dehydrogenase activity in vivo.
Url:
- https://api.istex.fr/document/13845390E7062D4A95C626A0BE88513D5D0742F8/fulltext/pdf
- https://api.istex.fr/document/90E866557803B321AE5B1B97A60F5B24F7952018/fulltext/pdf
DOI: 10.1016/0003-9861(86)90571-0
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000380
- to stream Istex, to step Curation: Pour aller vers cette notice dans l'étape Curation :000380
- to stream Istex, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :002E19
- to stream Main, to step Merge: Pour aller vers cette notice dans l'étape Curation :00F226
- to stream Istex, to step Corpus: Pour aller vers cette notice dans l'étape Curation :001B44
- to stream Istex, to step Curation: Pour aller vers cette notice dans l'étape Curation :001B44
- to stream Istex, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :002E18
- to stream Main, to step Merge: Pour aller vers cette notice dans l'étape Curation :00F225
Links to Exploration step
ISTEX:13845390E7062D4A95C626A0BE88513D5D0742F8Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Regulation of NADP-malate dehydrogenase in C4 plants: Effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems</title><author><name sortKey="Rebeille, F" sort="Rebeille, F" uniqKey="Rebeille F" first="F." last="Rebeille">F. Rebeille</name></author><author><name sortKey="Hatch, M D" sort="Hatch, M D" uniqKey="Hatch M" first="M. D." last="Hatch">M. D. Hatch</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:13845390E7062D4A95C626A0BE88513D5D0742F8</idno><date when="1986" year="1986">1986</date><idno type="doi">10.1016/0003-9861(86)90571-0</idno><idno type="url">https://api.istex.fr/document/13845390E7062D4A95C626A0BE88513D5D0742F8/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000380</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000380</idno><idno type="wicri:Area/Istex/Curation">000380</idno><idno type="wicri:Area/Istex/Checkpoint">002E19</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">002E19</idno><idno type="wicri:doubleKey">0003-9861:1986:Rebeille F:regulation:of:nadp</idno><idno type="wicri:Area/Main/Merge">00F226</idno><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:90E866557803B321AE5B1B97A60F5B24F7952018</idno><idno type="url">https://api.istex.fr/document/90E866557803B321AE5B1B97A60F5B24F7952018/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001B44</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001B44</idno><idno type="wicri:Area/Istex/Curation">001B44</idno><idno type="wicri:Area/Istex/Checkpoint">002E18</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">002E18</idno><idno type="wicri:doubleKey">0003-9861:1986:Rebeille F:regulation:of:nadp</idno><idno type="wicri:Area/Main/Merge">00F225</idno><idno type="wicri:Area/Main/Curation">00DF88</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Regulation of NADP-malate dehydrogenase in C4 plants: Effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems</title><author><name sortKey="Rebeille, F" sort="Rebeille, F" uniqKey="Rebeille F" first="F." last="Rebeille">F. Rebeille</name><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>Department de Biologie, Service de Radioagronomie, CEN-Cadarache, BP No. 1, 13115 St. Paul lez Durance</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">St. Paul lez Durance</settlement></placeName></affiliation></author><author><name sortKey="Hatch, M D" sort="Hatch, M D" uniqKey="Hatch M" first="M. D." last="Hatch">M. D. Hatch</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Division of Plant Industry, CSIRO GPO Box 1600, Canberra City, ACT 2601</wicri:regionArea><wicri:noRegion>ACT 2601</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Archives of Biochemistry and Biophysics</title><title level="j" type="abbrev">YABBI</title><idno type="ISSN">0003-9861</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1986">1986</date><biblScope unit="volume">249</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="164">164</biblScope><biblScope unit="page" to="170">170</biblScope></imprint><idno type="ISSN">0003-9861</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0003-9861</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Assay</term><term>Biochem</term><term>Biophys</term><term>Chloroplast</term><term>Dehydrogenase</term><term>Dhap</term><term>Edta</term><term>Electron flux</term><term>Enzyme activity</term><term>Ferredoxin</term><term>Final concentration</term><term>Final concentrations</term><term>High ratios</term><term>Inactivation</term><term>Initial rate</term><term>Intact chloroplasts</term><term>Light intensity</term><term>Maize</term><term>Mesophyll</term><term>Mesophyll chloroplasts</term><term>Nadp</term><term>Nadp ratio</term><term>Nadp ratios</term><term>Nadph</term><term>Nadph concentration</term><term>Nadpmdh</term><term>Oxidized</term><term>Oxidized thioredoxin</term><term>Photosynthesis</term><term>Photosynthetic metabolites</term><term>Present studies</term><term>Pyridine nucleotide</term><term>Redox</term><term>Redox state</term><term>Reduceable</term><term>Reduceable substrates</term><term>Thiol groups</term><term>Thioredoxin</term><term>Thioredoxin content</term><term>Thioredoxin redox state</term><term>Total amount</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Assay</term><term>Biochem</term><term>Biophys</term><term>Chloroplast</term><term>Dehydrogenase</term><term>Dhap</term><term>Edta</term><term>Electron flux</term><term>Enzyme activity</term><term>Ferredoxin</term><term>Final concentration</term><term>Final concentrations</term><term>High ratios</term><term>Inactivation</term><term>Initial rate</term><term>Intact chloroplasts</term><term>Light intensity</term><term>Maize</term><term>Mesophyll</term><term>Mesophyll chloroplasts</term><term>Nadp</term><term>Nadp ratio</term><term>Nadp ratios</term><term>Nadph</term><term>Nadph concentration</term><term>Nadpmdh</term><term>Oxidized</term><term>Oxidized thioredoxin</term><term>Photosynthesis</term><term>Photosynthetic metabolites</term><term>Present studies</term><term>Pyridine nucleotide</term><term>Redox</term><term>Redox state</term><term>Reduceable</term><term>Reduceable substrates</term><term>Thiol groups</term><term>Thioredoxin</term><term>Thioredoxin content</term><term>Thioredoxin redox state</term><term>Total amount</term></keywords><keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Maïs</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Activation and inactivation of NADP-malate dehydrogenase purified from Zea mays leaves were followed in a reconstituted system provided with thioredoxin poised in various redox states with dithiothreitol. The initial rate of activation or inactivation of NADP-malate dehydrogenase was proportional to the concentration of reduced or oxidized thioredoxin, respectively. The rate of inactivation was about 16 times that for activation at pH 7.4. Both activities increased when the pH was increased from 7.4 to 8.0. The redox potentials (E′0, pH 7) for the dithiol-disulfide systems of thioredoxin and NADP-malate dehydrogenase were estimated to be about −0.30 and −0.33 V, respectively. As would be predicted from these values, high proportions of active malate dehydrogenase were developed only in the presence of very high ratios of reduced to oxidized thioredoxin. Similarly, when pyridine nucleotide was included, a high degree of activation of malate dehydrogenase was only observed with high NADPHNADP ratios. These results confirm predictions based on models developed in earlier studies that the NADPH to NADP ratio as well as the thioredoxin redox state may be critical in determining the level of NADP-malate dehydrogenase activity in vivo.</div></front></TEI><double idat="0003-9861:1986:Rebeille F:regulation:of:nadp"><ISTEX><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Regulation of NADP-malate dehydrogenase in C4 plants: Effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems</title><author><name sortKey="Rebeille, F" sort="Rebeille, F" uniqKey="Rebeille F" first="F." last="Rebeille">F. Rebeille</name></author><author><name sortKey="Hatch, M D" sort="Hatch, M D" uniqKey="Hatch M" first="M. D." last="Hatch">M. D. Hatch</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:13845390E7062D4A95C626A0BE88513D5D0742F8</idno><date when="1986" year="1986">1986</date><idno type="doi">10.1016/0003-9861(86)90571-0</idno><idno type="url">https://api.istex.fr/document/13845390E7062D4A95C626A0BE88513D5D0742F8/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000380</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000380</idno><idno type="wicri:Area/Istex/Curation">000380</idno><idno type="wicri:Area/Istex/Checkpoint">002E19</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">002E19</idno><idno type="wicri:doubleKey">0003-9861:1986:Rebeille F:regulation:of:nadp</idno><idno type="wicri:Area/Main/Merge">00F226</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Regulation of NADP-malate dehydrogenase in C4 plants: Effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems</title><author><name sortKey="Rebeille, F" sort="Rebeille, F" uniqKey="Rebeille F" first="F." last="Rebeille">F. Rebeille</name><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>Department de Biologie, Service de Radioagronomie, CEN-Cadarache, BP No. 1, 13115 St. Paul lez Durance</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">St. Paul lez Durance</settlement></placeName></affiliation></author><author><name sortKey="Hatch, M D" sort="Hatch, M D" uniqKey="Hatch M" first="M. D." last="Hatch">M. D. Hatch</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Division of Plant Industry, CSIRO GPO Box 1600, Canberra City, ACT 2601</wicri:regionArea><wicri:noRegion>ACT 2601</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Archives of Biochemistry and Biophysics</title><title level="j" type="abbrev">YABBI</title><idno type="ISSN">0003-9861</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1986">1986</date><biblScope unit="volume">249</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="164">164</biblScope><biblScope unit="page" to="170">170</biblScope></imprint><idno type="ISSN">0003-9861</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0003-9861</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Assay</term><term>Biochem</term><term>Biophys</term><term>Dehydrogenase</term><term>Edta</term><term>Final concentration</term><term>High ratios</term><term>Inactivation</term><term>Initial rate</term><term>Nadp</term><term>Nadp ratio</term><term>Nadp ratios</term><term>Nadph</term><term>Nadpmdh</term><term>Oxidized</term><term>Oxidized thioredoxin</term><term>Present studies</term><term>Pyridine nucleotide</term><term>Redox</term><term>Redox state</term><term>Thiol groups</term><term>Thioredoxin</term><term>Thioredoxin redox state</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Assay</term><term>Biochem</term><term>Biophys</term><term>Dehydrogenase</term><term>Edta</term><term>Final concentration</term><term>High ratios</term><term>Inactivation</term><term>Initial rate</term><term>Nadp</term><term>Nadp ratio</term><term>Nadp ratios</term><term>Nadph</term><term>Nadpmdh</term><term>Oxidized</term><term>Oxidized thioredoxin</term><term>Present studies</term><term>Pyridine nucleotide</term><term>Redox</term><term>Redox state</term><term>Thiol groups</term><term>Thioredoxin</term><term>Thioredoxin redox state</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Activation and inactivation of NADP-malate dehydrogenase purified from Zea mays leaves were followed in a reconstituted system provided with thioredoxin poised in various redox states with dithiothreitol. The initial rate of activation or inactivation of NADP-malate dehydrogenase was proportional to the concentration of reduced or oxidized thioredoxin, respectively. The rate of inactivation was about 16 times that for activation at pH 7.4. Both activities increased when the pH was increased from 7.4 to 8.0. The redox potentials (E′0, pH 7) for the dithiol-disulfide systems of thioredoxin and NADP-malate dehydrogenase were estimated to be about −0.30 and −0.33 V, respectively. As would be predicted from these values, high proportions of active malate dehydrogenase were developed only in the presence of very high ratios of reduced to oxidized thioredoxin. Similarly, when pyridine nucleotide was included, a high degree of activation of malate dehydrogenase was only observed with high NADPHNADP ratios. These results confirm predictions based on models developed in earlier studies that the NADPH to NADP ratio as well as the thioredoxin redox state may be critical in determining the level of NADP-malate dehydrogenase activity in vivo.</div></front></TEI></ISTEX><ISTEX><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Regulation of NADP-malate dehydrogenase in C4 plants: Relationship among enzyme activity, NADPH to NADP ratios, and thioredoxin redox states in intact maize mesophyll chloroplasts</title><author><name sortKey="Rebeille, F" sort="Rebeille, F" uniqKey="Rebeille F" first="F." last="Rebeille">F. Rebeille</name></author><author><name sortKey="Hatch, M D" sort="Hatch, M D" uniqKey="Hatch M" first="M. D." last="Hatch">M. D. Hatch</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:90E866557803B321AE5B1B97A60F5B24F7952018</idno><date when="1986" year="1986">1986</date><idno type="doi">10.1016/0003-9861(86)90572-2</idno><idno type="url">https://api.istex.fr/document/90E866557803B321AE5B1B97A60F5B24F7952018/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001B44</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001B44</idno><idno type="wicri:Area/Istex/Curation">001B44</idno><idno type="wicri:Area/Istex/Checkpoint">002E18</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">002E18</idno><idno type="wicri:doubleKey">0003-9861:1986:Rebeille F:regulation:of:nadp</idno><idno type="wicri:Area/Main/Merge">00F225</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Regulation of NADP-malate dehydrogenase in C4 plants: Relationship among enzyme activity, NADPH to NADP ratios, and thioredoxin redox states in intact maize mesophyll chloroplasts</title><author><name sortKey="Rebeille, F" sort="Rebeille, F" uniqKey="Rebeille F" first="F." last="Rebeille">F. Rebeille</name><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>Departement de Biologie, Service de Radioagronomie, CEN-Cadarache, BP No. 1, 13115 St. Paul lez Durance</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">St. Paul lez Durance</settlement></placeName></affiliation></author><author><name sortKey="Hatch, M D" sort="Hatch, M D" uniqKey="Hatch M" first="M. D." last="Hatch">M. D. Hatch</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Division of Plant Industry, CSIRO, GPO Box 1600, Canberra City, ACT 2601</wicri:regionArea><wicri:noRegion>ACT 2601</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Archives of Biochemistry and Biophysics</title><title level="j" type="abbrev">YABBI</title><idno type="ISSN">0003-9861</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1986">1986</date><biblScope unit="volume">249</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="171">171</biblScope><biblScope unit="page" to="179">179</biblScope></imprint><idno type="ISSN">0003-9861</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0003-9861</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chloroplast</term><term>Dehydrogenase</term><term>Dhap</term><term>Electron flux</term><term>Enzyme activity</term><term>Ferredoxin</term><term>Final concentrations</term><term>Intact chloroplasts</term><term>Light intensity</term><term>Maize</term><term>Mesophyll</term><term>Mesophyll chloroplasts</term><term>Nadp</term><term>Nadp ratio</term><term>Nadph</term><term>Nadph concentration</term><term>Nadpmdh</term><term>Oxidized</term><term>Oxidized thioredoxin</term><term>Photosynthesis</term><term>Photosynthetic metabolites</term><term>Redox</term><term>Redox state</term><term>Reduceable</term><term>Reduceable substrates</term><term>Thioredoxin</term><term>Thioredoxin content</term><term>Thioredoxin redox state</term><term>Total amount</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Chloroplast</term><term>Dehydrogenase</term><term>Dhap</term><term>Electron flux</term><term>Enzyme activity</term><term>Ferredoxin</term><term>Final concentrations</term><term>Intact chloroplasts</term><term>Light intensity</term><term>Maize</term><term>Mesophyll</term><term>Mesophyll chloroplasts</term><term>Nadp</term><term>Nadp ratio</term><term>Nadph</term><term>Nadph concentration</term><term>Nadpmdh</term><term>Oxidized</term><term>Oxidized thioredoxin</term><term>Photosynthesis</term><term>Photosynthetic metabolites</term><term>Redox</term><term>Redox state</term><term>Reduceable</term><term>Reduceable substrates</term><term>Thioredoxin</term><term>Thioredoxin content</term><term>Thioredoxin redox state</term><term>Total amount</term></keywords><keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Maïs</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: NADP-malate dehydrogenase activity, the ratio of NADPH to NADP, and thioredoxin redox state in Zea mays chloroplasts were determined after various treatments. Following transfer from dark to light, NADP-malate dehydrogenase was activated more than 20-fold within 10 min while the proportion of pyridine nucleotide as NADPH increased from about 25 to 90%, and the proportion of thioredoxin in the reduced form increased from 20 to more than 90%, in less than 1 min. After transfer back to the dark, NADPH levels dropped very rapidly to the initial values recorded before illumination, while enzyme activity and reduced thioredoxin levels decreased more slowly. Addition of oxaloacetate or 3-phosphoglyerate to illuminated chloroplasts results in a decrease of about 70% in the activity of NADP-malate dehydrogenase, a 30% decrease in the level of NADPH, and a 25% decrease in the reduced thioredoxin content. Adding dihydroxyacetone phosphate and pyruvate had no effect. These results are considered in relation to the hypothesis that NADP-malate dehydrogenase activity in chloroplasts may be determined by factors regulating the ratio of NADPH to NADP as well as those influencing the redox state of thioredoxin.</div></front></TEI></ISTEX></double></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Asie/explor/AustralieFrV1/Data/Main/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 00DF88 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Curation/biblio.hfd -nk 00DF88 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Asie
|area= AustralieFrV1
|flux= Main
|étape= Curation
|type= RBID
|clé= ISTEX:13845390E7062D4A95C626A0BE88513D5D0742F8
|texte= Regulation of NADP-malate dehydrogenase in C4 plants: Effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems
}}
| This area was generated with Dilib version V0.6.33. |  |