Sentence examples for buffer exchanges were used from inspiring English sources

The samples received from enzyme purification and subsequent buffer exchanges were used without prior dilution, but protein concentration was determined to calculate enzyme activities.

The buffer exchange was performed using 2 flat sheet Pellicon 2 Biomax 10 modified PES mini cassettes with a 10 kDa MWCO and a filtration area of 0.1 m per cassette.

Slow-exchanging amide protons identified in the 2D 15N-1HSQCQC spectra recorded after the H2O buffer was exchanged for a D2O buffer were used in the structure calculated with the NOE distance restraints to generate hydrogen bonds for the final structure calculation as previously described in the literature (Chakravarty et al., 2009).

No buffers were used in this work to avoid their contributions to the hydrogen exchange rates.

Cell debris was removed by centrifugation at 20000  g for 10 min at 4°C, and a buffer exchange was carried out using Vivaspin centrifugal concentrators (molecular mass cut-off 50 000 Da) into gel-filtration buffer containing 0.02% DDM.

Buffer exchange was done three times by using ultracentrifugation (50,000 rpm for 20 min at 4 °C), with resuspension of the protein in the appropriate buffer and equilibration for 30 min at ambient temperature after each exchange.

PD 10 gel filtration columns (GE Healthcare) were used for buffer exchange for further experiments.

Protein Desalting Spin Columns (Pierce , Thermo Fisher Scientific Waltham, MA, USA) were used for buffer exchange of protein samples.

The GST tag was removed by on-column enzymatic cleavage using PreScission protease (GE Healthcare), and HiTrap Desalting columns (GE Healthcare) were used for buffer exchange (50 mM Hepes, pH 7.0, and 100 mM KCl).

PD-10 Desalting Columns (Amersham Biosciences, Uppsala, Sweden) were used for buffer exchange to PBS and H11 was sterilized by filtration using an Ultrafree-MC sterile 0,22 μm filter unit (Millipore, Jaffrey, NH).

Buffer exchange was repeated once.