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1.
Biol Trace Elem Res ; 198(2): 472-477, 2020 Dec.
Article in English | MEDLINE | ID: mdl-32034682

ABSTRACT

Zinc plays a major role in skin integrity, which can be affected by dromedary camels' hard life conditions. Deficiencies in some trace elements especially in zinc can explain susceptibility of this species to skin diseases. Compared with ruminants, camel is already known for his relatively low zincemia. In order to assess dromedary camels' skin zinc content, the present study was carried out in several provinces located in the south of Morocco where camel skin diseases are commonly observed. Zinc content in dromedary camel skin was determined using for the first time laser-induced breakdown spectroscopy (LIBS), method considered so far quick and simple with few or no sample processing. Collected data showed that zinc skin contents ranged between 115 ± 60 (for external side) and 94 ± 82 ppm (for internal side) with significant variability according to animals and to skin layers (external side versus internal side). Zinc skin content decreased from external to internal layers. Such preliminary results could be used to compare skin zinc nutritional level in healthy camels with those affected by skin diseases.


Subject(s)
Camelus , Zinc , Animals , Lasers , Morocco , Spectrum Analysis
2.
Comp Biochem Physiol B Biochem Mol Biol ; 131(3): 509-17, 2002 Mar.
Article in English | MEDLINE | ID: mdl-11959033

ABSTRACT

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.


Subject(s)
Camelus , Ceruloplasmin/isolation & purification , Animals , Ceruloplasmin/metabolism , Copper/metabolism , Electrophoresis, Polyacrylamide Gel , Hydrogen-Ion Concentration , Molecular Weight , Oxidoreductases Acting on CH-NH Group Donors/metabolism , Spectrophotometry
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