Dark modulation of NADP-dependent malate dehydrogenase and glucose-6-phosphate dehydrogenase in the chloroplast |
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Authors: | Renate Scheibe Louise E. Anderson |
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Affiliation: | University of Illinois at Chicago Circle, Department of Biological Sciences, Box 4348, Chicago, IL 60680 U.S.A. |
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Abstract: | The properties of the system which reverses light modulation of NADP-dependent malate dehydrogenase and glucose-6-phosphate dehydrogenase activity in pea chloroplasts were examined. A factor catalyzing dark modulation of these enzymes was found. This factor cochromatographed with thioredoxin in all systems used (Sephacryl S-200, Sephadex G-75, DEAE-cellulose). Inhibition of dithiothreitol-dependent modulation and of dark reversal by antibody against Escherichia coli thioredoxin further suggest that the dark factor is in fact thioredoxin. It appears that the reaction is the reverse of the previously described dithiothreitol-dependent thioredoxin-catalyzed modulation of enzymes. The limiting step in vitro seems to be the oxidation of thioredoxin during the dark period. |
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Keywords: | Dark modulation Thioredoxin Malate dehydrogenase Glucose-6-phosphate dehydrogenase (Pea chloroplast) |
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