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Crude extracts were prepared using glass beads as indicated in Methods and equal amounts of protein were incubated with substrate ACV.
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It employs free vibration analysis, response spectrum method and equal energy assumption for the estimation of maximum out-of-plane response.
The protein concentration of the samples was measured according to the Bradford method and equal amount of protein was subjected to filter assay.
For tissue samples total protein content of brain homogenates was determined by the BCA method and equal amounts (25 micrograms) were assayed and results are expressed as pg/mL/µg protein.
After extraction, protein concentration was measured according to the Bradford method and equal amounts of protein were separated on SDS-PAGE and transferred onto nitrocellulose membrane.
The amounts of proteins in the supernatants were measured using the BCA method, and equal amounts of proteins were used for further separations.
Lysate protein concentrations were determined using the Bradford method and equal amounts of protein were separated on 8 10% SDS-polyacrylamide gels.
Protein concentration was measured (BCA method) and equal amounts of protein from each sample were separated by SDS-PAGE and electrophoretically transferred to a nitrocellulose membrane (Bio-Rad Laboratories, HerCaliforniaifornia, USA).
The protein contents were determined with the Bradford method and equal amounts of cellular lysates were resolved by gradient (4-12%) sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE; Bio-Rad, Hercules, CA).
The observed specificity was excellent for all assays, ranging from 95.5% to 100% when compared with the reference method and equal to 100% when compared with a composite reference standard.
Total protein concentrations were determined by the Bradford method and equal amounts (30 μg) were separated on 10% SDS-PAGE, transferred to nitrocellulose membranes, and blocked for 1 h in TBST buffer (20 mM TRIS, pH 7.5; 500 mM NaCl; 0.5% Tween 20) containing 5% nonfat milk.
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