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Furthermore, we observe in Figure S3 (Supplementary data) only small differences between the spectra of the proteins (the transmembrane OprM and the membrane MexA proteins) solubilized in solution (with β-OG) and incorporated into the sponge phase, as observed for other proteins [59].
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Protoplasts were harvested by centrifugation at 1000 rpm for 5 min, washed three times using the resuspension solution, and then solubilized in the solution containing 0.16 M mannitol and 0.02 M CaCl2 · 2H2O.
The end product (RES4) of a step-wise Humeomic fractionation procedure applied to a humic acid from soil was successfully solubilized in alkaline solution and then separated by preparative HPSEC to provide six size fractions.
Cell lysates solubilized in Laemmli solution were subjected to SDS-PAGE on 8 or 10% resolving gels and immunoblotting as described [39].
All proteins were solubilized in a solution S1 of composition: 1% (w/w) β-octylglucoside (β-OG) (from Sigma), 100 mM NaCl, 50 mM Na2HPO4 pH 7.5, and 5% (v/v) glycerol.
Eluted peptides were vacuum dried before being solubilized in Switchoss Solution (0.1% (v/v) formic acid, 3% (v/v) acetonitrile).
The tissue samples were solubilized in Laemmli solution (62.5 mM Tris, pH 6.8, 10% glycerol, 2.3% SDS, 5% β-mercaptoethanol, with 0.1%E-64E-64and0.1%leupeptin antiproteolytictic factors).
The protein pellet was solubilized in a solution with 8-M urea, 4% CHAPS and 30 mM Tris and sonicated on ice (4 × 5 s).
In addition, samples were taken from the solution and centrifuged at 8,000 rpm for 10 min to remove the precipitate, and then the concentrations of curcumin still solubilized in the solution were determined.
Tissue was solubilized in a solution containing 2.5%% sodium lauryl sulfate (SDS) and 20%% sucrose made up in 15 mM Tris buffer, pH 8.3, on a shaking platform for 18 h at 80 °C.
Compound 2 (0.448 mmol, 130 mg) was solubilized in a solution of 5 mL BBr3 in CH2Cl2 (1 M) into a two-neck flask, which was completely closed and kept under magnetic agitation.
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