PAPAIN-PRODUCED FRAGMENTS OF HORSE γ- AND β-GLOBULIN ANTITOXINS

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Abstract
Preparations consisting mostly of γ- or β-globulin were obtained from a horse antiserum to diphtheria toxin by ammonium sulfate precipitation. These preparations were treated with papain and the digests separated on Sephadex G-100 columns. The γ-globulin digests were resolved into a major 3.4 S component and smaller minor components. The β-globulin digest contained similar fragments and, in addition, a major 5.0 S component. All fragments neutralized toxin, the most active being the β-globulin 5.0 S and 3.4 S fragments. The 3.4 S γ- and β-globulin fragments were univalent. The 5.0 S β-globulin fragment was divalent, and it could be reduced to 3.4 S subunits by treatment with 0.3 M 2-mercaptoethanol.