The Biological Role of Ceruloplasmin and Its Oxidase Activity

Abstract
A blue protein from the α2-globulin fraction of human serum which possessed oxidase activity was first reported by Holmberg (1) In 1944. It was named ceruloplasmin (Cp), meaning a blue (substance) from plasma, by Holmberg and Laurell (2, 3) In later papers describing the purification and other basic observations on Its chemical properties. Since Cp accounts for over 95% of the circulating copper in a normal mammal and fluctuates greatly In numerous disease and hormonal states, its study has excited the imagination of scientists who have generated several thousand papers on its chemistry and biology. Cp is an attractive protein for study also because, like serum albumin, it appears to be multifunctional, as the principal copper transport protein, as a molecule directly involved in iron mobilization from the Iron storage sites to the plasma via its ferroxidase activity and, possibly, as a regulator of circulating biogenic amine levels through its oxidase activity. Several recent reviews summarize the chemical and catalytic properties of Cp (See our review (4) for further references.).