Abstract

Human sera were fractionated by gel filtration in a new type of dextran gel, Sephadex G-200. The proteins were eluted in three main peaks. Analytical ultracentrifugation of the material in these peaks revealed decreasing sedimentation coefficients with increasing retention in the column. The distribution of some individual proteins was studied by paper electrophoresis, immunoelectrophoresis, and double diffusion in agar gel. In the first peak α 2-macroglobulin and α-β-lipoproteins were identified. The 7-S γ-globulin was found in the second peak and albumin and transferrin in the third peak. By serological titrations and density-gradient ultracentrifugation antibodies of the 19-S type were found in the first peak and those of the 7-S type in the second peak. It was concluded that the proteins migrated at a rate determined by their size and that this dextran gel acted as a molecular sieve.

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