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Two-Dimensional Electrophoresis of Serum Proteins

Abstract

A METHOD of zone electrophoresis in starch gels has recently been described by one of us1. The high degree of resolution obtained with this method when applied to serum appears to be due to the use of a supporting medium the pore size of which approaches the molecular dimensions of some of the proteins involved, so that resolution by molecular sizes is superimposed on resolution by free solution mobilities. Consequently the starch-gel electrophoretic separations result from a qualitatively different process from that involved in free-solution electrophoresis. A combination of the two electrophoretic processes at right-angles should therefore give a much greater degree of resolution than is possible with either separately. Such a two-dimensional electrophoretic system has been tested by us, using electrophoresis on filter paper as a close approximation to that occurring in free solution. The present communication illustrates the type of result which can be obtained; a detailed description of the method will be published later.

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References

  1. Smithies, O., Biochem. J., 61, 629 (1955).

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  2. Michaelis, L., Biochem. Z., 234, 139 (1931).

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  3. Smithies, O., and Walker, N. F., Nature, 176, 1265 (1955).

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SMITHIES, O., POULIK, M. Two-Dimensional Electrophoresis of Serum Proteins. Nature 177, 1033 (1956). https://doi.org/10.1038/1771033a0

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