Application of free-flow electrophoresis on proteomics.

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  • プロテオミクスの新技術―電気泳動とマススペクトロメトリー―フリーフロー電気泳動のプロテオミクスへの応用
  • フリーフロー デンキ エイドウ ノ プロテオミクス エ ノ オウヨウ

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The principle of free-flow electrophoresis (FFE) was first introduced by Barrolier (1958) and Hannig (1961). FFE provides a liquid-based separation in three different operating modes: zone electrophoresis-separation of particles (cells, organelles) due to their electrophoretic mobility, isotachphoresis-separation of proteins and peptides in pH step gradient and isoelectric focusing-separation of proteins and peptides due to their isoelectric point. The key feature of FFE technology is as follows. (i) The separation is performed continuously and enables us to obtain as much as hundreds of milligrams or even gram amounts pure substances. (ii) the separation is performed in a thin aqueous film without gels and enables us to collection of matrix-free fraction with high reproducibility. Therefore, FFE technology ensures that the separated samples are compatible with all downstream concentration procedures (e.g. ultrafiltration), whose enrichment allows to visualize less abundant proteins for subsequent 2-DE analysis and separate poor soluble proteins (e.g. membrane proteins) for subsequent SDS-PAGE. Moreover, FFE can be coupled with such analytical methods as liquid chromatography/mass spectrometry. In the field of proteomics, FFE is a highly versatile technology to support key applications due to prefractionation of samples.

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