Extraction of Proteins from Gels: A Brief Review

In this chapter we report the various methods that have been employed to elute proteins from gels

Biji T. Kurien; R. Hal Scofield


Scholarcy highlights

  • To recover a specific protein of interest from a gel, it has to be liberated out of the gel matrix that imprisons them
  • Free-flow electrophoresis is even more challenging with respect to the technical requirements compared to the traditional method of gel electrophoresis followed by protein elution
  • Proteins recovered from gels have been used in protein chemistry, proteolytic cleavage, determination of amino acid composition, polypeptide identification by trypsin digestion and matrix assisted laser desorption ionization-time of flight mass spectroscopy, as antigens for antibody production, identifying a polypeptide corresponding to an enzyme activity and other purposes
  • Protein yields ranging from nanogram levels to 100 μg have been obtained
  • Complete elution by passive diffusion has been achieved by crushing a gel slice with a small Teflon pestle in an elution buffer containing 0.1% sodium dodecyl sulfate and incubating the crushed gel fragments for 4 h and 16-24 h on a rotator

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