Sentence examples for using a salt gradient from inspiring English sources

Reconstituted mononucleosomes were assembled as described previously [3] using a salt gradient dialysis and Lowary and Widom '601' DNA.

The bound protein was eluted using a salt gradient of up to 1 M NaCl in 25 mM CAPS (pH 10) and, following concentration, the protein was loaded onto a preparative Superdex-200 26/60 column (GE Healthcare) pre-equilibrated in 20 mM Tris (pH 8) and 150 mM NaCl.

Elution using a salt gradient provides additional wash stringency prior to peak elution and results in improved purity.

Any approach that can improve the capture rate can be integrated to lower the detection limit, such as using a salt gradient, engineered pores, and a miniaturized system.

The peptides were eluted using a salt gradient (0 to 100%) between solvent A and solvent B (10 mM potassium phosphate buffer containing 25% acetonitrile, 350 mM KCl, pH 2.85).

Using WAX chromatography, the intact GAGs were separated using a salt gradient from 0.1 M to 1.0 M NaCl at a solution pD of 10.25 with UV detection at 215 nm and on-flow H NMR. Figure  7 shows the UV chromatogram (A) and on-flow NMR spectrum (B) for the separation of heparin and OSCS.

Peptides are displaced from strong-cation-exchange resin using a salt step gradient and subsequently bind to a second reverse-phase media.

Gal-1P was detected using a low salt gradient procedure: Gradient 1: 98% A and 2% B (−10 to 8 min), a linear increase of B to 30% (8 15 min), a linear increase of B to 50% (15 25 min), hold 50% A and 50% B (25 30 min), a linear decrease of B to 2% (30 35 min).

Classical ion-exchange chromatography using a linear salt gradient to elute the adsorbed protein at fixed pH is the most common method to separate product-related impurities during downstream processing of biopharmaceuticals.

Purified GAGs were injected onto the column (1mL/minute) and washed with 5 volumes of binding buffer to remove unbound molecules before bound GAGs were eluted using a continuous salt gradient (0 1M NaCl in binding buffer), 1.5mL fractions were collected at a flow rate of 1mL/min and elution measured at an absorbance wavelength of 256nm.

The protein was eluted using a linear salt gradient of buffer B supplemented with 2 M KCl.