[Isolation and physico-chemical properties of rat ceruloplasmin]

Ceruloplasmin was isolated and purified from albino rat blood serum. Relative molecular mass of the protein is 130 000. Electrophoresis of the protein preparations leads to a formation of the apo-protein devoid of the oxidase activity and migrating slower than the holo-protein. Leucine was found to be the N-terminal amino acid of the ceruloplasmin polypeptide chain. The amino acid composition and carbohydrate content of the protein were determined. The tryptic peptide maps of rat ceruloplasmin were compared to those of human protein. The properties of rat and human ceruloplasmin are discussed with respect to copper metabolism in animal body as well as in normal humans and patients with Wilson's disease.