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Cloning, Expression and Molecular Characterization of Glutathione Transferase P1-1 Gene from the Camel, Camelus dromedarius

Cloning, Expression and Molecular Characterization of Glutathione Transferase P1-1 Gene from the Camel, Camelus dromedarius

Farid S. Ataya,1,2,* Dalia Fouad,3,4 Ajamaluddin Malik,1 Nikolaos E. Labrou,5 Mohamed S. Daoud1,6 and Hesham M. Saeed7

1Department of Biochemistry, College of Science, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi Arabia 
2Molecular BiologyDepartment, Genetic Engineering Division, National Research Centre, 33 El-Bohouth St. (former El-Tahrir St.), P.O. 12622, Dokki, Giza, Egypt
3Department of Zoology, College of Science, King Saud University, P.O. 22452, Riyadh 11459, Saudi Arabia
4Department of Zoology and Entomology, Faculty of Science, Helwan University, Ein Helwan, Cairo, Egypt
5Laboratory of Enzyme Technology, Department of Biotechnology, School of Food, Biotechnology and Development, Agricultural University of Athens, 75 Iera Odos Street, GR-11855-Athens, Greece
6King Fahd Unit Laboratory, Department of Clinical and Chemical Pathology, Kasr Al-Ainy University Hospital, Cairo University, El-Manial, Cairo 11562, Egypt
7Department of Biotechnology, Institute of Graduate Studies and Research, Alexandria University, Alexandria, Egypt

*      Corresponding author:



In this study, we report the cloning, expression and characterization of the glutathione transferase isoenzyme P1-1 gene from Camelus dromedarius (CdGSTP1-1). The coding sequence was cloned using RT-PCR. Sequence analysis demonstrated significant differences between amino acid sequence of C. dromedarius and other mammalian GSTP1-1 enzymes. Phylogenetic relationship was studied with different organisms belonging to animal kingdom and revealed that CdGSTP1-1 is grouped with the enzyme from S. scrofa. The 3D homology model of CdGSTP1-1 showed similar fold and topology with the porcine GSTpi enzyme. Gene expression analysis in five camel tissues was examined employing real-time PCR. The highest level of transcripts was found in the camel testis, followed by liver, spleen, kidney and lung. CdGSTP1-1 was heterologously expressed in Eschericia coli BL21(DE3) as a ~24 kDa soluble protein and showed to be catalyticly active towards the model substrate 1-chloro-2,4-dinitrobenzene. The results of the present study provide new information into camelid evolution and give further insights into the diversity and complex enzymatic functions of GST superfamily.

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Pakistan Journal of Zoology


Vol. 52, Iss. 5, Pages 1631-2026


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