Abstract
In a study of 50 full-term newborns, we found serum levels of ceruloplasmin, its oxidase activity and specific oxidase activity (activity per unit mass of enzyme protein) which were significantly lower than in adult subjects (p<0.001). A significant correlation was obtained between the specific oxidase activity of the neonatal ceruloplasmin and the transferrin/alpha-fetoprotein ratio (p<0.01), which reflects the maturity of the fetal hepatocyte through its ability to synthesise fetal- and non-fetal-associated proteins. The lower specific oxidase activity of the ceruloplasmin in newborns would be due to a higher relative proportion of apoprotein, and/or other molecular forms with a poor copper content in the oxidase sites. This could be due to an inability to transfer copper into a common intracellular pool for holoceruloplasmin synthesis and biliary copper excretion. A high interindividual variability was found for the specific oxidase activity of the neonatal ceruloplasmin, and in the newborns with higher levels of ceruloplasmin this, from a catalytic point of view, is more similar to the adult form.
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