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The results show that carbonyl groups of the proteins increase during IEF in the presence of NaCl, and the proteins become more basic after refocusing IEF.
As Li+ ions were incorporated into the interlayer of BiOCl crystals, unique internal electric field (IEF) in BiOCl that trigger unusual photon avalanche (PA) UC phenomena accompanying with excitation field enhancement of Er3 + ions can be improved significantly, leading to the excellent UC enhancement.
Our series specifically reports the results of the IEF in the treatment of this uncommon complication.
The proteins were separated using liquid phase IEF in a Microrotofor cell and SDS PAGE.
The liquid phase IEF in the Microrotofor cell was conducted according to [31].
IEF in solution enables fractionation of proteins in their native state by isoelectric point (pI) because ampholytes are used to generate the pH gradient used for separation.
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Contamination of salts in IEF results in high conductivity, prolonged and poor focusing, electroosmosis, and thus poor resolution of proteins.
For each composite, 300 µg of protein were added to running buffer (8.1 M urea, 2 M thiourea, 4% CHAPS, 0.2% CA (Biolyte) (3 10), 2 mM TBP and 0.05 M DTT) and added to wells of isoelectric focusing (IEF) trays in PROTEAN IEF cell units.
40 The authors report significant decreases in IEF and increases in quality of life in women with SUI taking venlafaxine.
After equilibration, second dimension separation was performed on 15% SDS-polyacrylamide 13 × 9-cm gels with the focused sample embedded in 0.5% IEF agarose in a CriterionTM Cell (Bio-Rad) at 150 V for 1.5 h.
After completion of IEF, proteins in each strip were first reduced in 15 ml of a solution composed of 50 mM Tris HCl pH 6.8, 6 M Urea, 30% (v/v) glycerol, 2% (w/v) SDS, and 100 mM DTT, for 20 min in the dark at room temperature, then were alkylated in 15 ml of 50 mM Tris HCl pH 6.8, 6 M Urea, 30% (v/v) glycerol, 2% SDS, and 2.5% idoacetamide for 20 min at room temperature in the dark.
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