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Abstract                 Volume:4  Issue-12  Year-2016          Original Research Articles


Online ISSN : 2347 - 3215
Issues : 12 per year
Publisher : Excellent Publishers
Email : editorijcret@gmail.com

Partial Purification and Properties of Adenosine Triphosphatase (ATPase) From Leishmania tropica
Husain F.Hassan1* and Abeer Abbas Ali2
1Department of Biology, College of Science, University of Kirkuk, Iraq
2Department of Technical Analysis, Kirkuk Technical College, Northern Technical University, Iraq
*Corresponding author
Abstract:

The plasma membrane of cells contains enzymes whose active sites face the external medium rather than the cytoplasm. The adenosine tri phosphatase (ATP phosphohydrolase, EC 3.6.1.3.; ATPase) is membrane – bound enzyme which transport protons across the plasma membrane using ATP as an enegy source. In this work, we extracted the adenosine tri phosphatase from promastigotes of Leishmania tropica by chloroform treatment and purified by means of ammonium sulphate fractionation, gel filtration on sephadex G-200 and DEAE-Cellulose chromatography. Kinetic experiments demonstrated a biphasic linear lineweaver - burk relationship (km= 0.25 and 1.1 mM) thus revealing the existence of two substrate binding enzyme site and has an apparent molecular weight of 365000 dalton by gel filtration. The result of this study firmly provided the first direct evidence for the existence of Mg+2 - dependent ATPase in L. tropica, a fact which is of great interest from the phylogenetic point of view.

Keywords: ATPase,Leishmania tropica, gel filtration on sephadex G-200, DEAE-Cellulose chromatography.
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How to cite this article:

Husain F.Hassan, Abeer Abbas Ali. 2016. Partial Purification and Properties of Adenosine Triphosphatase (ATPase) From Leishmania tropica.Int.J.Curr.Res.Aca.Rev. 4(12): 54-63
doi: http://dx.doi.org/10.20546/ijcrar.2016.412.005