Preparation of Human Immunoglobulin by Caprylic Acid Precipitation

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Abstract
Caprylic acid was used to precipitate non immunoglobulin proteins from human plasma. The crude IgG present in the supernatant (which contained 26–29% of the total protein in terms of absorbance units or 78–87% of IgG by weight) was fractionated on DEAE-cellulose, to yield pure IgG as shown by disc electrophoresis, Immunoelectrophoresis and gel filtration. Pure IgG was free of plasmin and plasminogen and did not exhibit any fragmentation or aggregation during storage for periods up to 4 weeks at 40°C, and its anticomplementary activity was low. Antibodies to viral agents were recovered unchanged.