Young camel ceruloplasmin : purification and partial characterization

Abstract

Ceruloplasmin of a young camel (six months old) was isolated and purified using the single-step chromatography on amino ethyl-derivatized sepharose. The molecular mass of the protein, as estimated by non-reducing SDSelectrophoresis, was approximately 130,000 Da. The electrophoretic mobility of the young camel ceruloplasmin was slightly higher as compared to the human protein suggesting that the protein is compact and more acid. The copper content was estimated at 5.8 ± 0.3 atoms per molecule. The spectrocopic features included an absorption maximum at 610 nm, which could be attributed to type 1 copper. The EPR spectrum was completely devoid of any typical signal of type 2 copper. p-phenylendiamine oxidase properties of the young camel ceruloplasmin were determined: Km = 0.42 µM NADH/mn/mg Cp and Vmax = 0.93. Optimum pH for the activity was 5.7.