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The optimum pH was determined by measuring the PGL activity in buffered reaction mixtures with pH ranging from 7.0 to 11.0 (0.05 M glycine-NaOH buffer).
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A recent report found no manufactured enzyme to be contaminant-free and that levels of contamination varied among enzyme and buffer reaction lots [43].
Through variation of experimental conditions (temperature, pH, nature of buffer, reaction time) a selective and sensitive spectrofluorimetric batch method was developed for ampicillin determination.
Constructs were washed three times with PBS+1% Triton X-100, pelleted and resuspended in the methyltransferase buffer reaction.
This transient deficit in ATP (Fig. 9D solid line) was mostly matched by the ATP production from the creatine kinase ATP buffer reaction (Fig. 9D, dashed-dotted line).
The reaction mixture was then incubated at 30°C for 4 hours followed by heat inactivation at 65°C for 10 min. In both protocols, the sample buffer, reaction buffer, and enzyme mix were included in the GenomiPhi V2 kit.
Another control consisted of buffer reaction without protein.
A blank, constituting of modified IP buffer, reaction buffer and Ac-DEVD-AMC, was likewise incubated in parallel to the reaction mixtures.
A bicarbonate buffer reaction, similar to the function of the kidney, was added to account for proton balancing.
The absolute value of those kinetic constants in the ferritin system is very high, which determines the fast buffer reaction of the system.
The buffer reaction was not initially thought to be necessary until the requirement for balancing the protons in the interstitial space became apparent during network simulations.
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