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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 14 (1987), S. 113-124 
    ISSN: 1573-5079
    Keywords: NADP-malate dehydrogenase ; glutathione
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract NADP-malate dehydrogenase extracted from darkened leaves of the C3 plants pea, barley, wheat and spinach was activated by reduced glutathione, a monothiol, as well as by dithiothreitol (DTT). However, in the C4 plants maize and Flaveria trinervia, only dithiothreitol could effectively activate the enzyme. There was no activation of the maize enzyme and little or no activation of the F. trinervia enzyme by glutathione. The failure of glutathione to activate NADP-MDH in leaf extracts of maize and F. trinervia may indicate there is some difference in disulfide groups of the protein compared to the C3 plant enzyme. Both DTT and glutathione could activate NADP-malate dehydrogenase in a partially purified enzyme preparation from pea leaves with or without addition of partially purified thioredoxin. However, the required concentration of reductant was lower with addition of thioredoxin than in its absence. In extracts of C3 species and the partially purified pea enzyme the level of activation after 40 to 60 min under aerobic conditions was higher (up to twofold) with DTT than with glutathione. Under anaerobic conditions, the initial rate of activation was about twice as high with DTT as with glutathione, but the total activation after 40 to 60 min was similar. Ascorbate was totally ineffective as a reducing agent in activating NADP-MDH from C3 or C4 plants, possibly due to its more positive redox potential.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 14 (1987), S. 125-135 
    ISSN: 1573-5079
    Keywords: NADP-malate dehydrogenase ; leaf development ; C3 species ; nitrate assimilation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The activity of NADP-malate dehydrogenase (NADP-MDH) was determined in the developing first leaf of the C3 plants wheat, barley and pea. Light dependent activation of the enzyme was observed in all three species following rapid extraction and immediate assay. Maximum activity was obtained following extraction from preilluminated leaves and incubation on ice for 45 min in the presence of dithiothreitol. In all three species, maximum activity was obtained in the young leaf 4 days after emergence of the seedling (about 2.5 to 3 μmoles per milligram chlorophyll per min in wheat and barley, and 6 μmoles per milligram chlorophyll per min in pea). On a chlorophyll basis there was an approximate five-fold decrease in NADP-MDH activity as the leaf matured. A similar pattern was found for phospho-enolpyruvate carboxylase and NADP-malic enzyme which had maximum activity in younger leaf tissue. Similarly, the activity of nitrate reductase in wheat and barley was high in the young leaf and it rapidly declined as the leaf matured. In contrast, the capacity for photosynthesis was relatively low in the young leaf, reaching a maximum 6 to 8 days after seedling emergence. The pattern of change in activity of phosphoribulokinase, an enzyme of the reductive pentose phosphate pathway, was similar to that of photosynthesis. The results suggest NADP-MDH and phospho-enolpyruvate carboxylase have important function(s) in the young leaf, which are not directly linked to C3 photosynthesis, and which, in part, may be linked to nitrate assimilation and provision of malate to mitochondria.
    Type of Medium: Electronic Resource
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