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DNases have been classified into DNase I enzymes, which have an activity optimum at approximately pH 7.0 and require magnesium ions, and DNase II enzymes, which have a magnesium-independent activity optimum at approximately pH 5.0.
The profile is narrower and has a pH optimum at approximately pH 6.8, lower than the value of 7.4 found for the wild-type enzyme.
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The same conclusion was also reached for population genomics studies [ 28], which showed that it was more advantageous to sequence more individuals at low-coverage than fewer individuals at high-coverage, with an optimum obtained at approximately 1 x.
An optimum value was reached at approximately 120 degrees of freedom (edf) for the spatial trend function (Eq. 8.5).
An optimum point is reached at approximately 0.125 edges per pixel, implying a 12.5% chance for each 5 × 5 m region in the local area covered by an aerial image pixel to contain an edge.
Expression time trials showed that optimum HA-expression levels occurred at approximately 7 days post infiltration (dpi).
In fact, a diluted Ag+ concentration (ca. 10 μM) projected the quasi-1D nanoparticles growth and optimum at a concentration of approximately 20 μM.
For example, an optimum ratio for Ni/Fe was observed at approximately 20 wt% Ni for post-coated particles.
The recombinant leGSTp had a maximum activity at approximately pH 8.0, and its optimum temperature was 35 °C.
The pH optimum was approximately 5.5 to 6.0, and at these pHs Ca2+/CaM stimulated activity by about 70% and TFP inhibited activity by 35-60% in the presence of Ca2+/CaM.
The optimum temperature was not altered significantly by the mutations, and every mutant showed full activity at approximately 90°C, similar to the wild-type enzyme.
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