Activity of Glyceraldehyde-3-Phosphate Dehydrogenase-NADP in Developing Leaves of Light-Grown Dianthus chinensis L.

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Activity of Glyceraldehyde-3-Phosphate Dehydrogenase-NADP in Developing Leaves of Light-Grown Dianthus chinensis L.

Quantitative histochemical methods were used to measure glyceraldehyde-3-phosphate dehydrogenase-NADP activity in developing and mature leaves of Dianthus chinensis L. The activity values were compared on the basis of illumination of developing leaves, the maturity of stomata, and the activity of enzymes concerned with carbohydrate oxidation. Activity on a kilogram dry weight per hour basis inc...

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The Histochemical Demonstration of Glyceraldehyde-3-phosphate Dehydrogenase Activity

A histochemical method for demonstration of glyceraldehyde-3-phosphate dehydrogenation by tissues is described. The method utilizes Nitro BT as an indicator, glyceraldehyde-3-phosphate obtained from hydrolysis of commercially obtainable glyceraldehyde-3-phosphate diethylacetal (monobarium salt) as substrate, and (ethylenediamine)tetraacetic acid acid disodium as an activating agent in a medium ...

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Activation of Chloroplast NADP-linked Glyceraldehyde-3-Phosphate Dehydrogenase by the Ferredoxin/Thioredoxin System.

NADP-glyceraldehyde-3-P dehydrogenase of spinach (Spinacia oleracea) chloroplasts was activated by thioredoxin that was reduced either photochemically with ferredoxin and ferredoxin-thioredoxin reductase or chemically with dithiothreitol. The activation process that was observed with the soluble protein fraction from chloroplasts and with the purified regulatory form of the enzyme was slow rela...

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Glyceraldehyde-3-phosphate dehydrogenase is regulated by ferredoxin-NADP reductase in the diatom Asterionella formosa.

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Mechanism of glyceraldehyde-3-phosphate transfer from aldolase to glyceraldehyde-3-phosphate dehydrogenase.

The catalytic interaction of glyceraldehyde-3-phosphate dehydrogenase with glyceraldehyde 3-phosphate has been examined by transient-state kinetic methods. The results confirm previous reports that the apparent Km for oxidative phosphorylation of glyceraldehyde 3-phosphate decreases at least 50-fold when the substrate is generated in a coupled reaction system through the action of aldolase on f...

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ژورنال

عنوان ژورنال: Plant Physiology

سال: 1987

ISSN: 0032-0889,1532-2548

DOI: 10.1104/pp.84.4.1427