Abstract
The production of hormones by biotechnological approaches has contributed significantly to treatment of many diseases. DNA recombinant technology has facilitated production of new forms of insulin from many species and mammalian insulin to be used as a therapy for diabetic patients. In this study, proinsulin from Arabian camel was produced and characterized for the first time by recombinant technology. Recombinant camel proinsulin was cloned and expressed in Escherichia coli to be produced and characterized it in vitro. Camel proinsulin sequence was compared with human insulin sequences. Camel proinsulin is 5.8 kDa in size and includes 87 amino acids with highly conserved domains. Proinsulins are highly conserved enzymes in many mammals; camel proinsulin possesses 87.5% homology to human proinsulin by amino acid sequences. The C peptide chain is made up of a total of 35 amino acids of which 27 amino acids are identical and the remaining are variable. The three dimensional structure of camel proinsulin was deduced for molecule homology studies with human proinsulin. The results suggest that, camel proinsulin cDNA may be used as a specific probe for proinsulin studies with other organisms and may serve biotechnology field as a model for future comparative enzymatic, therapeutic and pharmaceutical studies.