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LDH-M has a lower Km and higher V max for pyruvate reduction than LDH-H (30).
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Bricker, D. K. et al. A mitochondrial pyruvate carrier required for pyruvate uptake in yeast, Drosophila, and humans.
As examples, analyses of the temperature dependence of Michaelis Menten (K′PYRm) and substrate inhibition (KsiPYR) constants for pyruvate, of the maximal rate of reaction (V′max), of the apparent Arrhenius activation energy (EA), and of the Gibbs free-energy change (ΔG‡) of lactate dehydrogenases from muscle of Atlantic cod Gadus morhua acclimated to 4 °C are described.
PKM2 isoform-specific deletion reveals a differential requirement for pyruvate kinase in tumor cells.
The imported carbon source required for pyruvate synthesis depends strongly on the available oxygen.
The estimated lower-quantification limit for pyruvate was between 16.96 and 20.55 pmol per 106 cells and a mean of these two values was used for calculating the lactate:pyruvate ratio for the missing data points.
Israelsen, W. J. et al. PKM2 isoform-specific deletion reveals a differential requirement for pyruvate kinase in tumor cells.
After the pyruvate producing strain was constructed, optimal culture conditions for pyruvate production were determined.
Thus construction of E. coli strains for pyruvate production involves introducing mutations that reduce utilization of pyruvate for cell growth and deletion of nonessential pathways through pyruvate metabolism.
d-f) the saturation curves for pyruvate with or without oxamate.
For FNLDH, oxamate inhibits the reaction competitively with pyruvate at pH 7.0, and substitutes for the role of pyruvate in the homotropic enzyme activation at pH 8.0, converting the sigmoidal saturation curve for pyruvate to a hyperbolic one (Figure 5d).
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