Results 271 to 280 of about 72,905 (323)
Some of the next articles are maybe not open access.
Apollo-NADP+: a spectrally tunable family of genetically encoded sensors for NADP+
Nature Methods, 2016NADPH-dependent antioxidant pathways have a critical role in scavenging hydrogen peroxide (H2O2) produced by oxidative phosphorylation. Inadequate scavenging results in H2O2 accumulation and can cause disease. To measure NADPH/NADP(+) redox states, we explored genetically encoded sensors based on steady-state fluorescence anisotropy due to FRET ...
Cindy V. Bui +8 more
openaire +3 more sources
Inhibition of NADP-malic enzyme activity by H2 S and NO in sweet pepper (Capsicum annuum L.) fruits.
Physiologia Plantarum : An International Journal for Plant Biology, 2019NADPH is an essential cofactor in many physiological processes. Fruit ripening is caused by multiple biochemical pathways in which, reactive oxygen and nitrogen species (ROS/RNS) metabolism is involved. Previous studies have demonstrated the differential
María A. Muñoz-Vargas +3 more
semanticscholar +1 more source
NADP regulates the light activation of NADP-dependent malate dehydrogenase
Planta, 1983The chloroplastic NADP-dependent malate-dehydrogenase (EC 1.1.1.82) activity is modulated by light and dark. The enzyme is activated upon illumination of intact or broken chloroplasts or by incubation with dithiothreitol, whereas dark has the opposite effect.
Jean-Pierre Jacquot +3 more
openaire +3 more sources
Binding of NAD and NADP dimers to NAD- and NADP-dependent dehydrogenases
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984Interaction of the electrolytically prepared dimers of nicotinamide adenine nucleotide, (NAD)2, and nicotinamide adenine nucleotide phosphate, (NADP)2, with lactate, alcohol, glyceraldehyde 3-phosphate, alpha-glycerophosphate, glutamate and glucose-6-phosphate dehydrogenase has been studied using the quenching of protein fluorescence, kinetics of ...
H. Klukanová, J. Kovár
openaire +3 more sources
Thio-NADP is not an antagonist of NAADP
Cell Biochemistry and Biophysics, 1998Nicotinic acid adenine dinucleotide phosphate (NAADP) is a metabolite of NADP, which can release Ca2+ from stores that are distinct from those activated by either cyclic ADP-ribose or inositol 1,4,5-trisphosphate (IP3). It has previously been suggested that thio-NADP is a specific antagonist of NAADP (Chini et al. [1995] J. Biol. Chem. 270, 3216-3223).
Dickey, DM +3 more
openaire +4 more sources
The Synthesis of Poly-L-Lysine-Succinyl-Nadp: An Analogue for Nadp/H
The International Journal of Artificial Organs, 1980Poly-L-lysine-succinyl-NADP, an analogue for nicotinamide adenine dinucleotide phosphate (NADP/H), has been synthesized by linking NADP/H to poly-L-lysine hydrobromide. This analogue (PL-SNP) was assayed with N, N dimethylaniline (DMA) in the presence of hepatic microsomal oxidase. A regeneration system of G-6-p and G-6-PD was used for reducing the PL-
Southard Wm, Sofer Ss, Wills Ra
openaire +3 more sources
Archives of Biochemistry and Biophysics, 1965
Abstract Chlorophyllin a catalyzes the photoreduction of NADP (and NAD to a lesser extent) in the presence of ascorbate as electron donor and NADP reductase as the coupling enzyme. Photosynthetic pyridine nucleotide reductase is inactive in the reaction and does not stimulate the reaction observed with NADP reductase.
Dorothy A. Limbach +2 more
openaire +3 more sources
Abstract Chlorophyllin a catalyzes the photoreduction of NADP (and NAD to a lesser extent) in the presence of ascorbate as electron donor and NADP reductase as the coupling enzyme. Photosynthetic pyridine nucleotide reductase is inactive in the reaction and does not stimulate the reaction observed with NADP reductase.
Dorothy A. Limbach +2 more
openaire +3 more sources
Complex formation by ferredoxin-NADP+ reductase with ferredoxin or NADP+
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1973Abstract Complex formation by ferredoxin-NADP + reductase (NADPH:ferredoxin oxidoreductase, EC 1.6.99.4) with ferredoxin was measured by the independent methods based on the changes of circular dichroism, fluorescence intensity and the chromatographic behavior on a Sephadex G-75 column of the two proteins after mixing.
openaire +3 more sources
Affinity labeling of spinach ferredoxin-NADP+ oxidoreductase with periodate-oxidized NADP+
Archives of Biochemistry and Biophysics, 1984Periodate-oxidized NADP+ (dialdehyde-NADP+) inactivated soluble ferredoxin-NADP+ oxidoreductase and combined covalently to the enzyme. This inactivation was first order with respect to dialdehyde-NADP+ and followed saturation kinetics, indicating that the enzyme initially forms a reversible complex with the inactivator.
Néstor Carrillo, Raquel Lia Chan
openaire +3 more sources