TY  - JOUR
T1  - Phylogenetic Analysis of Lysozyme C from the Scorpion <I>Mesobuthus eupeus</I> Venom Gland
AU - Eskandari, Ghafar AU - Khoonmirzaei, Nabiallah AU - Jolodar, Abbas 
JO  - Research Journal of Biological Sciences
VL  - 6
IS  - 1
SP  - 9
EP  - 11
PY  - 2011
DA  - 2001/08/19
SN  - 1815-8846
DO  - rjbsci.2011.9.11
UR  - https://makhillpublications.co/view-article.php?doi=rjbsci.2011.9.11
KW  - amino acids
KW  -anti-microbial protein
KW  -Iran
KW  -scorpion venom
KW  -Phylogenetic analysis
KW  -lysozyme C
AB  - Many studies have been carried out on peptides and genes encoding scorpion toxins from the venom of the scorpion <I>Mesobuthus eupeus</I>. The scorpion venom contains a diversity of bioactive peptides which could cause toxic effects and can be candidates for drug design and development. The anti-microbial lysozymes among them are of great value. Lysozymes are hydrolytic enzymes characterized by the ability to cleave the &beta;-(1, 4)-glycosidic bond between N-acetylmuramic acid and N-acetyl-D-glucosamine in a peptidoglycan layer, the major bacterial cell wall polymer. The total RNA was extracted from venom glands of <I>Mesobuthus eupeus</I> species of Kuzestan. cDNA was synthesized with extracted total RNA as template and modified oligo (dT) as primer. In order to amplify cDNA encoding a Lys-C peptide, semi-nested RT-PCR was performed with the specific primers followed by sequencing of the amplified fragment. The full-length cDNA sequence contains a 438 nucleotide open reading frame encoding a peptide of 144 amino acids with molecular weight of 16.702 kDa. A putative 22-residue signal peptide was identified. Based on the phylogenetic tree of MesoLys-C and c-type lysozyme of East Mediterranean <I>M. eupeus</I> it is concluded that <I>M. eupeus</I> of Khuzestan and East Mediterranean <I>M. eupeus</I> belong to different subspecies.
ER  -