History of electrophoresis
The history of electrophoresis for molecular separation and
Before Tiselius
Early work with the basic principle of electrophoresis dates to the early 19th century, based on
Experiments by
Methods of optical detection of moving boundaries in liquids had been developed by August Toepler in the 1860s; Toepler measured the schlieren (shadows) or slight variations in optical properties in inhomogeneous solutions. This method combined with the theoretical and experimental methods for creating and analysing charged moving boundaries would form the basis of Tiselius's moving-boundary electrophoresis method.[6]
Development and spread of the Tiselius apparatus
The apparatus designed by Arne Tiselius in 1931 enabled a range of new applications of electrophoresis in analyzing chemical mixtures. Its development, significantly funded by the Rockefeller Foundation, was an extension of Tiselius's earlier PhD studies. With more assistance from the Rockefeller Foundation, the expensive Tiselius apparatus was built at a number of major centers of chemical research.
After Tiselius
By the late 1940s, new electrophoresis methods were beginning to address some of the shortcomings of the
Zone electrophoresis found widespread application in biochemistry after Oliver Smithies introduced starch gel as an electrophoretic substrate in 1955. Starch gel (and later polyacrylamide and other gels) enabled the efficient separation of proteins, making it possible with relatively simple technology to analyze complex protein mixtures and identify minute differences in related proteins.
Despite the development of high-resolution electrophoresis methods, the accurate control of parameters such as pore size and stability of polyacrylamide gels was still a major challenge in the 20th century. This technical problem was finally solved in the early 2000s with the introduction of a standardized polymerization time for polyacrylamide gels, making it possible for the first time to fractionate physiological concentrations of highly purified metal ion cofactors and associated proteins in quantitative amounts for structure analysis.[7]
Widespread application
Since the 1950s, electrophoresis methods have diversified considerably, and new methods and applications are still being developed as affinity electrophoresis, capillary electrophoresis, electroblotting, electrophoretic mobility shift assay, free-flow electrophoresis, isotachophoresis, preparative native PAGE, and pulsed-field gel electrophoresis.[7]
See also
- Electrophoresis
- Electrophoresis (journal)
- History of biochemistry
- History of chromatography
- History of electrochemistry
- History of gel electrophoresis
- History of molecular biology
Notes
- ^ Malhotra, P. (2023). Analytical Chemistry: Basic Techniques and Methods. Springer, ISBN 9783031267567. p. 346.
- .
- ^ Michov, B. (1995). Elektrophorese: Theorie und Praxis. De Gruyter, ISBN 9783110149944. p. 405.
- ^ Reuss, F.F. (1809). "Sur un nouvel effet de l'électricité galvanique". Mémoires de la Société Impériale des Naturalistes de Moscou. 2: 327–37.
- ^ Vesterberg, pp. 4-5
- ^ Vesterberg, p. 5
- ^ ISBN 9783110761641.
References
- Vesterberg, Olof (1989). "History of Electrophoretic Methods", Journal of Chromatography, volume 480, pp. 3–19.