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The physiochemical and immunological characterization of Gm (1) antibodies from normal human serum
The mol. wt and charge characteristics of Gm(1) antibodies from normal human serum were studied by gel filtration and DEAE- anion exchange chromatography. The effect on anti-Gm(1) activity, of incubating individual antisera with disulphide reducing agents, and with anti-IgG or anti-IgM immunoabsorbents were also studied. The results demonstrate the existence of a low molecular weight IgM protein with anti-Gm(1) activity.
The mol. wt and charge characteristics of Gm(1) antibodies from normal human serum were studied by gel filtration and DEAE- anion exchange chromatography. The effect on anti-Gm(1) activity, of incubating individual antisera with disulphide reducing agents, and with anti-IgG or anti-IgM immunoabsorbents were also studied. The results demonstrate the existence of a low molecular weight IgM protein with anti-Gm(1) activity.