Suggestions(1)
Exact(1)
The protein solution after buffer exchange was subjected to the peptide-cleavage process.
Similar(59)
Buffer exchange was repeated once.
The eluted protein was concentrated, and a buffer exchange was performed with 25 mM phosphate buffer containing 10 µM FAD.
Imaging was initiated as soon as the buffer exchange was complete.
The exchanged buffer exchanged was 0.01 × PBS/0.01 mM DTT/2.5 mM imidazole/0.1% glycerol.
In a second approach nickel affinity purified PsOep23 was subjected to buffer exchange in 20 mM sodium phosphate pH 7.0, 8 M urea using Amicon centrifugal filters (MWCO 10 kDa, Merck).
To generate partially-purified, enriched unlinkase activity fractions via cation-and-anion exchange chromatography (Fraction CA), RSW was subjected to cation-exchange chromatography (SP Sepharose FF, GE Healthcare), and proteins were eluted from the column using increasing concentrations of NaCl in unlinkase buffer.
The purified protein was subjected to buffer-exchange into 50 mM ammonium bicarbonate containing 5 mM EDTA, pH 8.5, using a 3,000 MW cutoff Amicon Ultra (Fisher Scientific) centrifugal filter unit and concentrated to 1 mg/mL.
The recovered IDEPT agent was subjected to an additional buffer exchange step using an additional Zeba Spin Desalting Column.
The cell supernatant was subjected to 3 rounds of buffer exchange (10 fold dilution each time) using a large scale diafiltration apparatus versus 5 mM phosphate buffer at pH 7 containing 100 mM NaCl.
The resulting dialyzed MIF-II fraction was subjected to ion exchange chromatography column of DEAE-cellulose previously equilibrated with 10 mM potassium phosphate buffer, pH 7.5.
Write better and faster with AI suggestions while staying true to your unique style.
Since I tried Ludwig back in 2017, I have been constantly using it in both editing and translation. Ever since, I suggest it to my translators at ProSciEditing.

Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com