Characterization of
recombinant Arabian camel (Camelus dromedarius)
insulin
Abdulaziz M. Al-Swailem*, Mohamed B. Al-Fageeh, Essam
J. Alyamani,
Maher M. Shehata and Turki A. Al-Shammari
Biotechnology Research Center, Natural Resources and
Environment Research Institute, King Abdulaziz City for
Science and Technology, Riyadh, Saudi Arabia
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.