Immunochemical studies of crystalline human ceruloplasmin and derivatives.

Previous immunochemical investigations of ceruloplasmin have been primarily concerned with the assay of this substance in human sera and its localization by the technique of immunoelectrophoresis. The proteins used in the preparation of antisera appear to have been impure or poorly defined. The ready availability of crystalline human ceruloplasmin (I, 2) prompted us to study its immunochemical properties as an adjunct to its physicochemical characterization (3). The lability of this protein to rather mild treatment is reflected in a pronounced modification of its immunochemical properties. Most of these changes appear to be related to a partial loss of copper from the molecule.