Published March 31, 2015
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Fig. 3 in Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate
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Fig. 3. Competition assays. Stern–Volmer representation of NAD-ME1 fluorescence quenching by fumarate in the presence of 15 mM L-malate (A) and NAD-ME1 fluorescence quenching by L-malate in the presence of 4 mM fumarate (B). The excitation wavelength was set at 295 nm and the fluorescence was recorded at 344 nm. All values were corrected for buffer spectra and dilution.
Notes
Published as part of Tronconi, Marcos Ariel, Wheeler, Mariel Claudia Gerrard, Martinatto, Andrea, Zubimendi, Juan Pablo, Andreo, Carlos Santiago & Drincovich, María Fabiana, 2015, Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate, pp. 37-47 in Phytochemistry 111 on page 40, DOI: 10.1016/j.phytochem.2014.11.009, http://zenodo.org/record/10487825
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- Journal article: 10.1016/j.phytochem.2014.11.009 (DOI)
- Journal article: urn:lsid:plazi.org:pub:D8457224FFB9FFB4D6563D460F2EFFDC (LSID)
- Journal article: https://zenodo.org/record/10487825 (URL)