Purification and partial characterization of camel (Camelus Dromedarius) ceruloplasmin

被引:6
作者
Essamadi, AK
Bengoumi, M
Zaoui, D
Faye, B
Bellenchi, GC
Musci, G
Calabrese, L
机构
[1] CIRAD EMVT, Programme Prod Anim, F-34032 Montpellier, France
[2] Univ Hassan, Lab Biochim, Fac Sci & Tech Settat, Settat 26000, Morocco
[3] IAV, Lab Biochim Clin, Rabat, Morocco
[4] Univ Chouaib Doukkali, Lab Biochim, Fac Sci Jadida, El Jadida, Morocco
[5] Univ Rome 3, Dipartemento Biol, Rome, Italy
[6] Univ Messina, Dipartimento Chim Organ & Biol, Messina, Italy
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 2002年 / 131卷 / 03期
关键词
camel; ceruloplasmin; chromatography; electrophoresis; molecular weight; oxidase activity; purification;
D O I
10.1016/S1096-4959(02)00030-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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-phenylendiamime oxidase were determined as K-m = 0.42 mM and V-max = 0.93 muM NADH/mn/mg Cp. The optimum pH for the activity was 5.7. (C) 2002 Elsevier Science Inc. All rights reserved.
引用
收藏
页码:509 / 517
页数:9
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