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While at 100 mM NaCl DBD is still able to access a stoichiometry of 3 1 on any of the substrates used, at 150 mM NaCl it is clear that only two molecules of DBD can bind at saturation.
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To examine the substrate specificity of mAP, the following substrates were used at a final concentration of 0.5 mM: pNPP, D-glucose 1-phosphate, O-phosphoethanolamine, phosphoenolpyruvate, phytic acid, paraoxon, and methyl parathion in 50 mM DEA buffer (pH 9.0).
The following hydrolase substrates were used at concentrations of 6 mM: 4-methylumbelliferyl-phosphate for acid phosphatase activity, 4-methylumbelliferyl-β-D-glucuronide for β-glucuronidase activity, and 4-methylumbellifery-α-D-mannopyranoside (Sigma) for α-mannosidase activity.
All substrates were used at a final concentration of 5 g/liter.
Substrates were used at a saturating concentration, which was determined experimentally (data not shown).
All substrates were used at two different concentrations (5 and 1 mM) and a fixed amount of cosolvent was used.
aAll substrates were used at a final concentration of 10 mg/ml, except salecan (5 mg/ml).
This was determined under optimal conditions for enzymatic catalysis as determined above, except that choline-containing substrates were used at concentrations close to their Km (between 1 and 2 Km).
GaAsBi epilayers were grown on semi-insulating GaAs substrates using MBE at 360°C to 390°C, while keeping the As/Bi atomic species ratio close to unity.
When fluorite and perovskite-structured ceramic materials were used as substrates, H2 yields were higher than when an inert Al2O3 substrate was used at 700 800 °C.
The substrate was used at 10 µM and the protein at 0.2 µM.
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