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  2. Desalting and buffer exchange - Wikipedia

    en.wikipedia.org/wiki/Desalting_and_buffer_exchange

    Desalting and buffer exchange both entail recovering the components of a sample in whatever buffer is used to pre-equilibrate the small, porous polymer beads (resin). Desalting occurs when buffer salts and other small molecules are removed from a sample in exchange for water (with the resin being pre-equilibrated in water).

  3. Diafiltration - Wikipedia

    en.wikipedia.org/wiki/Diafiltration

    Diafiltration for Desalting or Buffer Exchange; Mobius Ultra/ Diafiltration Solutions This page was last ...

  4. Protein purification - Wikipedia

    en.wikipedia.org/wiki/Protein_purification

    Because of the nature of the separating mechanism, pH, buffer type, buffer concentration, and temperature all play important roles in controlling the separation. Ion exchange chromatography is a very powerful tool for use in protein purification and is frequently used in both analytical and preparative separations.

  5. Dialysis (chemistry) - Wikipedia

    en.wikipedia.org/wiki/Dialysis_(chemistry)

    Dialysis is the process used to change the matrix of molecules in a sample by differentiating molecules by the classification of size. [6] [7] It relies on diffusion, which is the random, thermal movement of molecules in solution (Brownian motion) that leads to the net movement of molecules from an area of higher concentration to a lower concentration until equilibrium is reached.

  6. Ammonium sulfate precipitation - Wikipedia

    en.wikipedia.org/wiki/Ammonium_sulfate_precipitation

    Ammonium sulfate is an inorganic salt with a high solubility that disassociates into ammonium (NH + 4) and sulfate (SO 2− 4) in aqueous solutions. [1] Ammonium sulfate is especially useful as a precipitant because it is highly soluble, stabilizes protein structure, has a relatively low density, is readily available, and is relatively inexpensive.

  7. Dithiothreitol - Wikipedia

    en.wikipedia.org/wiki/Dithiothreitol

    DTT is a reducing agent; once oxidized, it forms a stable six-membered ring with an internal disulfide bond.It has a redox potential of −0.33 V at pH 7. [1] The reduction of a typical disulfide bond proceeds by two sequential thiol-disulfide exchange reactions and is illustrated below.

  8. Sample preparation in mass spectrometry - Wikipedia

    en.wikipedia.org/wiki/Sample_preparation_in_mass...

    In LC-MS the desalting/concentration is realised with a pre-column, in off-line measurements reversed phase micro columns are used, which can be used directly with microliter pipettes. Here, the peptides are eluted with the spray solution containing an appropriate portion of organic solvent.

  9. Fast protein liquid chromatography - Wikipedia

    en.wikipedia.org/wiki/Fast_protein_liquid...

    Fast protein liquid chromatography (FPLC) is a form of liquid chromatography that is often used to analyze or purify mixtures of proteins. As in other forms of chromatography, separation is possible because the different components of a mixture have different affinities for two materials, a moving fluid (the mobile phase) and a porous solid (the stationary phase).