Exact(1)
One unit of α-amylase activity was defined as the amount of enzyme needed to release 1 μmol maltose equivalent reducing groups per minute The pH and temperature range at which the recombinant α-amylase was active were determined using soluble starch as substrate.
Similar(59)
Cdc42 activation was determined using an Active Cdc42 Pull-Down and Detection Kit (Thermoscientific) as per manufacturer's instructions.
Selected "active" compounds were determined using empirical thresholds for their associated Docking Score (DS) and eModel Score (eM), where any active compound had a DS ≤ −7 kcal/mol and an eM ≤ −50 kcal/mol [44, 69, 70].
The structures of the active compounds were determined using spectroscopic methods and their drug-likeness evaluated using Lipinski parameters.
While possible active site were determined using LIGSITEcsc and CASTp web servers simultaneously [ 16- 18].
Protein active sites were determined using (Conserved Domain Architecture Retrieval Tool (CDART) [ 37] and the conserved domain database (CDD) [ 38].
Active Cdc42 levels were determined using the Active Cdc42 Pull-Down and Detection Kit (Pierce-Thermo Fisher Scientific, Waltham, MA, USA).
The nuclear and cytoplasmic contents of active β-catenin were determined using the "Nuclear Localization" algorithm in the ImageStream software.
Active state onsets were determined using sigmoid fits of the membrane potential traces after removal of spikes (Fig. 4 a ).
Plasma concentrations of enrofloxacin and its active metabolite ciprofloxacin were determined using a validated high-performance liquid chromatography method (HPLC) with fluorescence detection.
Total glucose-dependent insulinotropic polypeptide and active GLP-1 were determined using commercially available human ELISA kits according to the manufacturer's guidelines (Millipore).
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