Light activation of nadp malate dehydrogenase in a reconstituted chloroplastic system
โ Scribed by Jean Vidal; Jean Pierre Jacquot; Pierre Gadal
- Publisher
- Elsevier Science
- Year
- 1980
- Tongue
- English
- Weight
- 667 KB
- Volume
- 19
- Category
- Article
- ISSN
- 0031-9422
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
Dithiothreitol activation of spinach leaf NADP malate dehydrogenase is mediated by protein factors that have been partially purified by chromatography on DEAE cellulose. Evidence for their intrachloroplastic localization has been obtained.
The light-dependent inhibition of glucose-6-phosphate dehydrogenase (EC 1.1.1.49), the key enzyme of the oxidative pentose phosphate cycle, can be gradually abolished in an illuminated reconstituted spinach chloroplast system by increasing the concentration of NADP(+). The inhibition caused by the e
In a preparation of soluble components from isolated spinach (Spinecia oleracea L.) chloroplasts, the activity of ribulose-l,5-bisphosphate carboxylase (EC 4.1.1.39) is strongly increased by 6-phosphogluconate or by NADPH at pH 8.0. When the thylakoid system is added to these soluble components (rec