Sentence examples for residue solution from inspiring English sources

Specifically residue characteristics of stable residue solution such that; pH of 5.5 9.0, sodium adsorption ratio (SAR) of ≤ 7, exchangeable sodium percentage (ESP) of ≤ 9.5, residual sodium carbonate (RSC) of ≤ 1.25, electrical conductivity (EC) of < 4 mS/cm.

Add 250 µl cDNA Binding Buffer to each sample, mix well and load onto cDNA Filter Cartridge; Spin 1 min at 10,000×g, discard flow-through; Wash once with 500 µl Wash Buffer, spin additional 2 min to remove residue solution and transfer cartridge to cDNA Elution Tube; Elute cDNA with 20 µl of H2O 55°CC preheated).

Add 350 µl cRNA Binding Buffer and 250 µl of 100% Ethanol, mix well and load onto cRNA Filter Cartridge; Spin ∼1 min at 10,000×g, discard flow-through; Wash once with 500 µl Wash Buffer, spin additional 2 min to remove residue solution and transfer cartridge to cRNA Elution Tube; Elute cRNA with 100 µl of H2O.

The remaining residue solution was transferred into a 100-mL volumetric flask.

Fig. 6 a UV/Vis absorption spectra of the initial TCH solution and the residue solutions obtained by filtration using MWCNTs/GO and PDDA-MWCNTs/GO membranes.

The adsorption system consisted of 1.0 mL hydrolysis lignin residues solution (40 mg/mL), 0.5 mL Cel solution, and 0.5 mL buffer for control that was without LS addition or 0.5 mL LS solution (4.5 mg/mL).

Further, it was purified by vacuum suction filtration to remove residue in solution, and GQDs powders were obtained by evaporation.

0.2 mL of the coffee processing residue extracted solution was combined with 15.8 mL of DI water, 1 mL of Folin Ciocalteau (FC) reagent, and 3 mL of sodium carbonate in a 40-mL test tube.

Therefore, the observed conformation of phosphorylated Ser158 in the crystalline state would be different from the conformation of this residue in solution.

Water (40 mL) was added to the residue, the solution was made basic (KOH, pH 14), and was extracted with dichloromethane (4 × 50 mL).

Even though Ser/Ser would have a p Ka value of approximately 9.0, which is 4.0 units lower than a free serine residue in solution (p Ka=13), it is well known that protein active sites can change the p Ka values of ionizable groups on catalytic residues compared with their values in free solution [ 45].