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Therefore, interaction of arsenic trioxide with HSA and BSA was investigated in aqueous solution at physiological conditions using a constant protein concentration and various drug contents.
This study was designed to examine the interaction of HSA with oseltamivir phosphate (OP) and oseltamivir carboxylate (OC) in aqueous solution at physiological conditions, using a constant protein concentration and various drug contents.
This study was designed to examine the interaction of BSA with 5-Fluorouracil (5-FU) and two of its derivatives; FUPAE and FUPAP at physiological conditions, using a constant protein concentration and various drug contents.
Inhibition of recombinant domain binding to CSPG was performed mainly as the above described ELISA analysis, but using a constant protein concentration (5 µg/ml) pre-mixed with increasing amounts of soluble CSA (0.5 400 µg/ml).
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We determined the binding affinity of GST-ARN127(25) and GST-Htt exon 1(25) for F-actin by using a constant amount of protein (16 nM for ARN127, 150 nM for Htt exon 1) mixed with increasing amounts of F-actin (Fig. 1C, D).
Therefore, using a constant resin volume normalizes for protein content in this assay.
Moreover, our knowledge of these two proteins is incomplete: P0C0B0 is an uncharacterized protein whereas Q8GW13 is a putative c- myc binding protein, which is suggestive of how these two proteins are represented using a constant amino acid characteristic from AAIndex [ 13] and a dynamic characteristic [ 14– 14].
For immunoblotting, proteins (10 μg) were first separated with 15% polyacrylamide gels using a constant voltage (100 V) in a Mini PROTEAN II system (BioRad, Hercules, CA, USA).
Initial analysis was conducted using a constant comparative approach [ 18].
Analyses were conducted using a constant comparative approach.
Data were analysed using a constant comparison approach.
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