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Ceruloplasmin has been isolated from sheep plasma by a procedure involving two chromatographic steps and (NH4)2SO4 fractionation. The ovine protein is similar to ceruloplasmins from other species previously described (human, bovine), having a single chain of about 125 Kdal with a very high degree of homology in the amino acid composition. It differs, however, from human and bovine ceruloplasmin because of its lower copper content and its higher specific enzyme activity. The oxidase activity as well as the spectroscopic properties were found to be pH range 5-8 with a pH optimum for activity of 6.3.
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