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  2. Electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Electrophoresis

    The method spread slowly until the advent of effective zone electrophoresis methods in the 1940s and 1950s, which used filter paper or gels as supporting media. By the 1960s, increasingly sophisticated gel electrophoresis methods made it possible to separate biological molecules based on minute physical and chemical differences, helping to ...

  3. Gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis

    Unlike denaturing methods, native gel electrophoresis does not use a charged denaturing agent. The molecules being separated (usually proteins or nucleic acids ) therefore differ not only in molecular mass and intrinsic charge, but also the cross-sectional area, and thus experience different electrophoretic forces dependent on the shape of the ...

  4. Electrophoresis (journal) - Wikipedia

    en.wikipedia.org/wiki/Electrophoresis_(journal)

    Electrophoresis is a peer-reviewed scientific journal covering all aspects of electrophoresis, including new or improved analytical and preparative methods, development of theory, and innovative applications of electrophoretic methods in the study of proteins, nucleic acids, and other compounds.

  5. Category:Electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Category:Electrophoresis

    Electrophoresis is a method of moving charged particles through a medium by using an electric field induced by electrodes. It is also used to separate molecules with different physical characteristics using electrical charges.

  6. History of electrophoresis - Wikipedia

    en.wikipedia.org/wiki/History_of_electrophoresis

    The method spread slowly until the advent of effective zone electrophoresis methods in the 1940s and 1950s, which used filter paper or gels as supporting media. By the 1960s, increasingly sophisticated gel electrophoresis methods made it possible to separate biological molecules based on minute physical and chemical differences, helping to ...

  7. Two-dimensional gel electrophoresis - Wikipedia

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

    Two-dimensional gel electrophoresis, abbreviated as 2-DE or 2-D electrophoresis, is a form of gel electrophoresis commonly used to analyze proteins. Mixtures of proteins are separated by two properties in two dimensions on 2D gels. 2-DE was first independently introduced by O'Farrell [ 1 ] and Klose [ 2 ] in 1975.

  8. Affinity electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Affinity_electrophoresis

    This method differs from the traditional agarose gel electrophoresis by utilizing a higher voltage to facilitate a shorter run time as well as yield a higher band resolution. Other factors included in developing the technique of rapid agarose gel electrophoresis are gel thickness, and the percentage of agarose within the gel.

  9. Isoelectric focusing - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_focusing

    The gradient is established before adding the particles of interest by first subjecting a solution of small molecules such as polyampholytes with varying pI values to electrophoresis. The method is applied particularly often in the study of proteins, which separate based on their relative content of acidic and basic residues, whose value is ...

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