Purification and partial characterization of camel (Camelus Dromedarius) ceruloplasmin
| Autor: | Abdel Khalid Essamadi, Lilia Calabrese, Giovani Musci, Gian Carlo Bellenchi, Mohammed Bengoumi, Bernard Faye, Driss Zaoui |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
endocrine system
Camelus Physiology chemistry.chemical_element Biochemistry law.invention Sepharose law Animals L50 - Physiologie et biochimie animales Electron paramagnetic resonance Molecular Biology Oxidoreductases Acting on CH-NH Group Donors Oxidase test Chromatography biology Molecular mass Chemistry Ceruloplasmin Hydrogen-Ion Concentration Copper Molecular Weight Electrophoresis Spectrophotometry biology.protein Electrophoresis Polyacrylamide Gel Specific activity |
| Zdroj: | Comparative Biochemistry and Physiology. Part B, Biochemistry and Molecular Biology |
| ISSN: | 1096-4959 |
| DOI: | 10.1016/s1096-4959(02)00030-1 |
| Popis: | Adult and young camel ceruloplasmin (Cp) were isolated and purified using the single-step chromatography on amino ethyl-activated sepharose. There are no differences between the adult and the young camel protein. The molecular mass of the protein, as estimated by SDS-PAGE (denaturant conditions), was approximately 130 000 Da. The electrophoretic mobility of camel Cp is slightly higher as compared to human and sheep protein suggesting that the camel Cp is homogeneous, compact and more acid. The copper content was estimated to be 5.8±0.3 atoms per molecule. The spectrocopic feature includes 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 the type 2 copper. The kinetic parameters of the adult camel Cp for the specific activity as p -phenylendiamine oxidase were determined as K m =0.42 mM and V max =0.93 μM NADH/mn/mg Cp. The optimum pH for the activity was 5.7. |
| Databáze: | OpenAIRE |
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