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C4519
Sigma
Ceruloplasmin human
lyophilized powder, oxidase 30-75 units/mg protein
| CAS Number: | 9031-37-2 |
| EC Number: | 232-868-3 |
| MDL number: | MFCD00130766 |
Description
| Analysis Note | Protein determined by biuret |
| Biochem/physiol Actions | Ceruloplasmin (Cp), the principal carrier of copper in plasma, is thought to be involved in oxidative modification of lipoproteins and participate in the acute phase reaction to stress. Cp is an effective antioxidant for a variety of radicals and has a potent peroxidase activity to decompose hydrogen peroxide in the presence of reduced glutathione. It inhibits the peroxidase activity of myeloperoxidase in a concentration-dependent manner and shows selective binding to myeloperoxidase in vitro. This suggests that ceruloplasmin may participate in the clearance and inactivation of myeloperoxidase in vivo. At physiological (micromolar) concentrations it was found to inhibit relaxation of rabbit aorta induced by endothelium-dependent agonists like acetylcholine or ADP. However, it was found ineffective toward vasodilation due to direct stimulation of smooth muscle cells by nitroglycerin. |
| Unit Definition | One unit will cause a ΔA550 of 0.01 per min using N,N-dimethyl-p-phenylenediamine as substrate at pH 5.5 and 37 °C, in a 7 mL reaction volume. |
| Physical form | Pale blue powder containing sodium chloride and sodium acetate |
Properties
| form | lyophilized powder |
| mol wt | mol wt ~135 kDa |
| composition | Protein, ~30% |
| copper content | 1.0-2.5 μg/mg protein |
| Gene Information | human ... CP(1356) |
| storage temp. | −20°C |
Safety
| Hazard Codes | B |
| WGK Germany | 3 |
References
| reference | Mukhopadhyay, C.K., Fox, P.L., Ceruloplasmin copper induces oxidant damage by a redox process utilizing cell-derived superoxide as reductant. Biochemistry 37, 14222, (1998) |
| Fox, P.L., Structure, oxidant activity, and cardiovascular mechanisms of human ceruloplasmin. Life Sci. 56, 1749, (1995) | |
| Atanasiu, R.L., Direct evidence of ceruloplasmin antioxidant properties. Mol. Cell Biochem. 189, 127-135, (1998) | |
| Kim, I.G., Park, S.Y., Requirement of intact human ceruloplasmin for the glutathione-linked peroxidase activity. FEBS Lett. 437, 293, (1998) | |
| Segelmark, M., Binding and inhibition of myeloperoxidase (MPO): a major function of ceruloplasmin?. Clin. Exp. Immunol. 108, 167, (1997) | |
| Cappelli-Bigazzi, M., Ceruloplasmin impairs endothelium-dependent relaxation of rabbit aorta. Am. J. Physiol. 273, (1997) |
