Abstract
The Chromatographic and gel filtration properties of human and swine serum have been compared using DEAE-cellulose and Sephadex G-200. Elution positions of the proteins have been determined using immunoelectrophoretic and agar gel diffusion analyses of every third effluent fraction. The elution positions of 14 well-characterized human serum proteins have been determined, and are compared with the elution positions of their probable swine serum counterparts. Comparative electrophoretic mobilities of 13 human and 14 swine serum proteins have been determined from immunoelectrophoretograms of the DEAE-cellulose fractions. The mobilities of the protein analogs are similar but with a trend toward electrophoretically slower mobilities for the swine serum proteins. The apparent molecular weights of several human and swine serum proteins were determined on Sephadex G-200 using whole serum and immunoelectrophoretograms of the effluent fractions as a means of assessing the void volume ( V o ) of the column and elution positions ( V) of the proteins. The molecular weights of the swine serum proteins are not significantly different from their human serum counterparts. The serum of both species was found to contain, in addition to α 2-macroglobulin, an additional macroglobulin with α 2 mobility.
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