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'A' is the maximum activity reached for larvae of a particular genotype and 'TA' is the time taken to reach maximum activity A. n indicates number of larvae.
'A' is the maximum activity reached for larvae of a particular genotype and 'TA' is the time taken to reach maximum activity, as diagrammed in Figure 5. Data represent mean ± s.e.m. n indicates number of larvae.
Aspartate aminotransferase from E. coli catalyzed the reaction involving aromatic amino acids at a rate of approximately 20%% of the maximum activity reached with l-aspartate, and the same enzyme from B. linens catalyzed the transamination reactions with the participation of various aromatic amino acids six to ten times less efficiently than reactions involving l-aspartate.
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The predicted value was verified experimentally, and the maximum enzyme activity reached 492 U/ml.
The maximum xylanase activity reached 16.11 U/mL after 144 h cultivation in the 15-L scaled fermenter.
Maximum promoter activity reached 450% at 16 hours compared with the controls (P < 0.001).
At 25°C, refolding was relatively slow, with the maximum 70% activity reached at pH 8.0 after seven days, and this activity could be maintained for a couple of days.
Specifically Tg hcrt ChR2-EYFP) larvae displayed a 25% increase in Tg hcrt ChR2-EYFPity larvaereachedisplayedstimulation and reached this maximum activity level 25% faster than sincreaseontrols.
When the pH was below 3.0 and above 8.0, only 30%40%% of the maximum activity was reached.
The EC50 (median effective concentration) values were calculated by determining the concentration by which 50% of maximum activity was reached using the sigmoidal fit equation.
The maximum activity was reached for different substrate compositions: at high xylose content for xylanase, and at low xylose content for the four cellulolytic activities for which the maximum was reached at different glucose/inducer ratio, depending also on the inducer choice.
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