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- W2091180984 abstract "The evolution of NADP-dependent malate dehydrogenase (MDH) activity was examined during the greening of primary leaves of Phaseolus vulgaris. The enzyme was present in material grown in darkness; upon illumination, the specific activity reached a level two to six times higher than of etiolated material. During the same time, NAD dependent MDH activity remained unchanged whereas the level of NADP dependent G-3P-DH increased tenfold. After the dark-light transition, D-threo-chloramphenicol had no effect on the evolution of enzyme actvities. This suggests that the enhancement of the catalytic power of these chloroplastic enzymes does not result from de novo protein synthesis but more probably from the activation, under light control, of pre-existing molecules. L'évolution de l'activité de la MDH à NADP a été suivie au cours verdissement des feuilles primordiales de Phaseolus vulgaris. L'enzyme est détectée dans le matériel maintenu à l'obscurité; l'exposition á la lumière permetd'atteindre une activité spécifique de 2 à 6 fois supérieure à celle du matériel étoilé. Durant la même période, la MDH à NAD reste stable alors que le niveau de la G-3P-DH à NADP augmente de 10 fois.Au cours de la transition obscurité-lumière, le D-thréo-chloramphénicol est sans effet sur l'accroissement d'activité de la MDH à NADP et de la G-3P-DH. Ceci suggère que l'augmentation du pouvoir catalytique de ces biocatalyseurs chloroplastiquesne résulte pas de la synthése de nouvelles protéines enzymatiques mais plutôt de l'activation, contrôlée par la lumière, de molecules préexistantes." @default.
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- W2091180984 date "1977-03-01" @default.
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- W2091180984 title "Etude de l'evolution de la malate deshydrogenase a NADP durant le verdissement des feuilles de Phaseolus vulgaris L" @default.
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- W2091180984 doi "https://doi.org/10.1016/0304-4211(77)90188-2" @default.
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