@article{Maharjan_2015, title={Characterization of Heat Shock Protein (HSP 70) Sequence in Leishmania donovani}, volume={20}, url={https://www.nepjol.info/index.php/JIST/article/view/13914}, DOI={10.3126/jist.v20i1.13914}, abstractNote={<p>Heat shock protein HSP70 is the highly conserved protein along the kinetoplastid phylogenetic spectrum. A full length <em>hsp70 </em>gene was amplified, cloned and sequenced. The protein sequence was aligned and phylogentic tree was constructed. The <em>Leishmania donovani </em>HSP70 protein sequence (653 amino acids) is slightly larger than the Human HSP70 protein sequence (641 amino acids) with 72% identity. The putative protein sequence is 98%, 97%, 96% and 92% identical to <em>L. major, L. infantum</em>, <em>L. tarentolae </em>and <em>L. braziliensis </em>respectively. Evolutionary relationship showed that kinetoplastid parasites are closely related to the human compared to prokaryotes, <em>E. coli</em>.</p><p>Journal of Institute of Science and Technology, 2015, <strong>20(1)</strong>: 82-86</p>}, number={1}, journal={Journal of Institute of Science and Technology}, author={Maharjan, Mahendra}, year={2015}, month={Nov.}, pages={82–86} }