Molecular-sieve chromatography and electrophoresis in polyacrylamide gels.
1. The absolute electrophoretic mobilities of eight proteins have been measured at pH8.76, I 0.05, in polyacrylamide gels of 20 different compositions at 10 degrees C. 2. The partition coefficients of these proteins have been determined chromatographically under the same conditions by using columns of granulated polyacrylamide gel prepared simultaneously. 3. The electrophoretic mobilities are an exponential function of the gel concentrations when the latter are corrected for water uptake. The constants of this function have been determined by curvefitting methods. They have been shown to be related to the free solution mobility and to the mean molecular radius respectively. 4. The reduced mobilities have been shown to be a linear function of the partition coefficients by statistical analyses. 5. The physical significance of the relation between electrophoretic mobility and chromatographic phase distribution in gel media is discussed in the context of these results.
D000178:Acrylamides; D000179:Acrylates; D002850:Chromatography, Gel; D003201:Computers; D004586:Electrophoresis; D005782:Gels; D008962:Models, Theoretical; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis; D014867:Water
D000178:Acrylamides; D000179:Acrylates; D005782:Gels; D011506:Proteins; D014867:Water