from Part D - Hydrodynamics
Published online by Cambridge University Press: 05 November 2012
Historical review
1920s
M. Smoluchowski and E.Hückel were the first to elaborate the theory of electrophoresis for thin and thick double layers. D. C. Henry provided a theory for the electrophoresis of spherical polyions that was valid for double layers of arbitrary thickness. In the Henry model, charge distribution within the sphere is assumed to be spherically symmetric, and ion relaxation is ignored. In the 1950s a number of investigators (J. Th. G. Oberbeek, F. Booth, P. H. Wiersma) studied the effect of ion relaxation on the electrophoretic mobility of spheres containing a centrosymmetric charge distribution.
1930
A. Tiselius presented a new technique for studying the electrophoretic properties of proteins. He showed that sharp electrophoretic moving boundaries of ionised molecules could be obtained in U-shaped quartz glass tubes and that the protein boundary could be detected with UV light. A. Tiselius described moving boundaries corresponding to albumin, α-, β-, and γ-globulin in serum.
1940s
T. Wieland and E. Fischer proposed the use of filter paper as a supporting medium for electrophoresis. Simplicity of construction, relative cheapness and compactness, and the requirement of much less than 1mg of protein for analytical or diagnostic purposes popularised paper electrophoresis.
1950s
O. Smithies obtained good resolution of proteins using starch gels. Electrophoresis with molecular sieving of a gel gave a much higher resolution than electrophoresis in free solution. In this decade, many materials (like strips of cellulose acetate, agarose) were introduced as supports for electrophoresis.
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