Claim · model-written summary
NADPH activated partially purified NADP-linked dehydrogenase.
- Treatment
- NADPHe0
- Outcome
- Activation of the NADP‐linked dehydrogenasee0
- Direction
- Activatione0
- Qualifier
- after its partial purification by ammonium sulfate fractionatione0
Not reportedTaxonMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleComparatorSettingValue
Verbatim
e0“Activation of the NADP‐linked dehydrogenase could also be attained by NADPH after its partial purification by ammonium sulfate fractionation”
Title
B. Müller; I. Ziegler; H. Ziegler European Journal of Biochemistry 1969. doi:10.1111/j.1432-1033.1969.tb00581.x
Other claims from this paper (12)
- Intervention effect Irradiation of green leaves or isolated chloroplasts rapidly and reversibly increased NADP-linked phosphoglyceraldehyde dehydrogenase activity.
- Mechanism The increase in NADP-linked enzyme activity was closely connected with non-cyclic photosynthetic electron flow.
- Association The light-induced increase was accompanied by decreased NAD-linked enzyme activity.
- Mechanism Dehydrogenase, rather than kinase, limited the measured overall reaction rate.
- Mechanism Dark-enzyme activation to light-enzyme form was not due to nonspecific reduction of reactive-center disulfide groups.
- Intervention effect Dithiothreitol restored only chloroplast isolation-related activity loss.
- Intervention effect NADPH specifically activated the basic enzyme.
- Mechanism Maximal activation required the basic enzyme to be fully reduced.
- Intervention effect Dithiothreitol plus NADPH activated the enzyme as strongly as light in vivo.
- Association Activation rate followed a sigmoidal response across NADPH concentrations.
- Association Basic-enzyme activity and activation ability differed in temperature sensitivity at 52°–60°.
- Mechanism The authors propose that NADPH acts allosterically to shift the enzyme toward an NADP-dependent form.