Electrophoresis of Normal Serum on Paper Treated with 0.01 Albumin

Electrophoresis of Normal Serum on Paper (K20) Treated with 0.01 °Jo Albumin 

Impregnation of the paper with alumina is reported for lipoproteins (B15, D2). Some authors have accentuated the disadvantages of the paper substrate in order to obtain some specific effect (D15), but in practice the results in work on serum proteins were small. Rather than complicating the problem by specific adsorption, a new and neutral substrate showing neither physical nor ion exchange adsorption seems to be the ideal goal. 

The shorter migration distance on paper than in free solution has been explained on the basis of a longer migration path along the tortuous capillaries of the paper (A8, D15, K22), with a field actually smaller than that calculated from the potential measured at the ends of the strip. It seems impossible to make absolute mobility measurements on paper, although relative mobilities may be obtained for clinical use (M22). 

Both the solvent and the solutes of the buffer solution must be discussed in relation to their functional properties. The pH is important in 

Solvent. Water is the usual solvent, but because it evaporates very easily some workers (D15) have used glycerol or analogous substances to reduce the vapor tension. These, however, have higher viscosities than water and will affect the mobility u of the migrating particle according to the equation 

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