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Peptide mapping is a critical method for evaluating the purity of complex substances such as proteins.
In the present study, three techniques based on different principles namely differential scanning calorimetry (DSC), the mass balance (MB) method based on high pressure liquid chromatography (HPLC) and coulometric titrimetry (CT) were compared in evaluating the purity of ferulic acid CRM for the first time.
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The HPLC and MS were used to evaluate the purity of the peptide and to check the peptide sequence, respectively.
To evaluate the purity of the generated acid and base during the performance and to confirm the capacity of both synthesized and commercial BPM regarding their efficiency to dissociate water into its ions, certain important parameters such as electrical conductivity, salinity, sodium ion, and chloride ion concentrations were analyzed.
We first evaluated the purity of the ghost samples, confirming that only erythrocyte membranes and Maurer's cleft were present without contamination by other parasite components.
To evaluate the purity of myocyte preparation, we used Tile Scanning Function (Leica Confocal) to examine the whole cover glass (22 mm diameter) after cells were subjected to immunostaining.
HPLC and mass spectrometry were used to characterize and evaluate the purity of the oligopeptide [ 23].
Histone 1 and glyceraldehyde-3-phosphate dehydrogenase were used to evaluate the purity of nuclear and cytoplasmic fractions, respectively, and served as lane load controls.
To evaluate the purity of the extracted DNA, absorbance ratios at 260 nm/230 nm (DNA / humic acids) and 260 nm/280 nm (DNA / protein) were determined (see Tables 2 and 3).
All PCR products were purified and separated in 1% agarose gel to evaluate the purity of the amplified DNAs and determine their size.
Through current finger printing technology, one can not only confirm the identity of established cell lines and identify new cell lines, but also evaluate the purity of a cell culture [ 3].
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