Purification and partial characterization of camel (Camelus dromedarius) ceruloplasmin

Essamadi Abdel Khalid, Bengoumi Mohammed, Zaoui Driss, Faye Bernard, Bellenchi Gian Carlo, Musci Giovani, Calabrese Lilia. 2002. Purification and partial characterization of camel (Camelus dromedarius) ceruloplasmin. Comparative Biochemistry and Physiology. Part B, Biochemistry and Molecular Biology, B (131) : 509-517.

Résumé : 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 clectrophoretic 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 I copper. The EPR spectrum was completely devoid of any typical signal of the type 2 copper. The kinetic parameters of the adult carnel Cp for the specific activity as p-phenylendiaimne oxidase were determined as Km=0.42 mM and Vmax=0.93 µM NADH/mn/mg Cp. The optimum pH for the activity was 5.7.

Classification Agris : L50 - Physiologie et biochimie animales

Auteurs et affiliations

• Essamadi Abdel Khalid, Université Hassan 1 (MAR)
• Bengoumi Mohammed, IAV Hassan II (MAR)
• Zaoui Driss, Université Chouaïb Doukkali (MAR)
• Faye Bernard, CIRAD-EMVT-PPA (FRA)
• Bellenchi Gian Carlo, Universita degli studi Roma tre (ITA)
• Musci Giovani, Universita di Messina (ITA)
• Calabrese Lilia, Universita degli studi Roma tre (ITA)

Source : Cirad - Agritrop (https://agritrop.cirad.fr/489848/)

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