Purification and partial characterization of camel (Camelus Dromedarius) ceruloplasmin.
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 130000 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 spectroscopic 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 microM NADH/mn/mg Cp. The optimum pH for the activity was 5.7.
Essamadi
Abdel Khalid
AK
Laboratoire de Biochimie, Université Hassan 1er, Faculté des Sciences et Techniques de Settat, BP 577, 26000, Settat, Morocco.
Bengoumi
Mohamed
M
Zaoui
Driss
D
Faye
Bernard
B
Bellenchi
Gian Carlo
GC
Musci
Giovani
G
Calabrese
Lilia
L
D000818:Animals; D002162:Camelus; D002570:Ceruloplasmin / Q000302:isolation & purification* / Q000378:metabolism; D003300:Copper / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism; D013053:Spectrophotometry
D003300:Copper; D002570:Ceruloplasmin; C022345:4-phenylenediamine oxidase; D000587:Oxidoreductases Acting on CH-NH Group Donors