Ceruloplasmin is an enzyme which catalyzes the oxidation of P-phenylenediamine by oxygen to purple-colored compound.
This enzyme is a blue-colored metalloprotein with an absorbance maximum at 605nm and specific absorptivity of 0.068XliterXg-1Xcm-1.
The protein migrates electrophoretically as analpha 2 globulin and contains 0.355 percent copper. Ceruloplasmin is a glycoprotein, containing 8 to 10 sialic acid residues per mol, for which relative molecular masses varying from 132, 000 to 162, 000 have been reported.
Before the enzyme properties of ceruloplasmin were discovered by Holmberg and Laurell, the protein was of interest as one of the "acute phase reaction" proteins present in serum. Ceruloplasmin is of most interest clinically because of its relation to Wilson´s disease. Ceruloplasmin level in serum is a significant sex difference, with the level in women some 20, percent higher than that in man.
The liver is the scurce of the protein enzyme present in plasma.
The level at birth is about 20 percent of that seen in adults.
We attempt to introduce and establish more rapid completion of ceruloplasmin determination based on kinetic method using a Gilford 203-S automatic chemistry analyzer.
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