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  2. Isoelectric point - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_point

    The isoelectric point (pI, pH(I), IEP), is the pH at which a molecule carries no net electrical charge or is electrically neutral in the statistical mean. The standard nomenclature to represent the isoelectric point is pH(I). [1] However, pI is also used. [2] For brevity, this article uses pI.

  3. Protein precipitation - Wikipedia

    en.wikipedia.org/wiki/Protein_Precipitation

    The isoelectric point (pI) is the pH of a solution at which the net primary charge of a protein becomes zero. At a solution pH that is above the pI the surface of the protein is predominantly negatively charged and therefore like-charged molecules will exhibit repulsive forces.

  4. Two-dimensional gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Two-dimensional_gel...

    The two dimensions that proteins are separated into using this technique can be isoelectric point, protein complex mass in the native state, or protein mass. [citation needed] The separation by isoelectric point is called isoelectric focusing. Thereby, a pH gradient is applied to a gel and an electric potential is applied across the gel, making ...

  5. Isoelectric focusing - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_focusing

    Isoelectric focusing (IEF), also known as electrofocusing, is a technique for separating different molecules by differences in their isoelectric point (pI). [ 1 ] [ 2 ] It is a type of zone electrophoresis usually performed on proteins in a gel that takes advantage of the fact that overall charge on the molecule of interest is a function of the ...

  6. George B. Walden - Wikipedia

    en.wikipedia.org/wiki/George_B._Walden

    George B. Walden (February 18, 1895 - August 6, 1982) was a chemist who worked for Eli Lilly and Company on the mass production of insulin. He discovered isoelectric precipitation, which solved a major problem and led to the mass production of insulin.

  7. Protein adsorption - Wikipedia

    en.wikipedia.org/wiki/Protein_adsorption

    Proteins with isoelectric point (pI) above physiological conditions have a positive charge and proteins with pI below physiological conditions have a negative charge. The net charge of the protein, determined by the sum charge of its constituents, results in electrophoretic migration in a physiologic electric field.

  8. Zeta potential titration - Wikipedia

    en.wikipedia.org/wiki/Zeta_potential_titration

    The iso-electric point is one such property. The iso-electric point is the pH value at which the zeta potential is approximately zero. At a pH near the iso-electric point (± 2 pH units), colloids are usually unstable; the particles tend to coagulate or flocculate. Such titrations use acids or bases as titration reagents.

  9. Difference gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Difference_gel_electrophoresis

    The three samples are mixed and loaded onto IEF (isoelectric focusing chromatography) for first dimension and the strip is transferred to a SDS PAGE.After the gel electrophoresis, the gel is scanned with the excitation wavelength of each dye one after the other, so each sample can be seen separately (if we scan the gel at the excitation wavelength of the Cy3 dye, we will see in the gel only ...