Physical and chemical analyses reveal modifications in ceruloplasmin after specific treatments, suggesting structural changes.
Crystalline ceruloplasmin was substantially freed of sialic acid by the action of neuraminidase. Sequential treatment of asialoceruloplasmin with galactose oxidase and tritiated borohydride resulted in the incorporation of tritium into at least 4 residues of D-galactose of the protein molecule.
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Morell et al. (1966) studied this question.
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