Abstract
Objective:
The adenosine triphosphatase (ATP phosphohydrolase, EC 3.6.1.3.;ATPase) is a membrane -bound enzyme which transport protons across the plasma membrane using ATP as an energy source.
Methods:
The adenosine triphosphatase (ATPase ; EC: 3.6.1.3) was extracted from membrane preparations of adult Fasciola hepatica by chloroform treatment and purified by means of ammonium sulphate fractionation, gel filtration on sephadex G-200 and DEAE- Cellulose chromatography.
Results:
The molecular weight was calculated to be 305.000 dalton by gel filtration. Kinetic experiments demonstrated a biphasic linear lineweaver - burk relationship (km=0.142 and 1.66 mM) thus revealing the existence of two substrate binding enzyme sites.
Conclusion:
In our study revealed that partial inhibition of Mg2+ dependent purified enzyme by oligomycin suggest the absence of mitochondrial ATPase in F. hepatica. (Turkiye Parazitol Derg 2014; 38: 26-31)
Keywords: ATPase, Fasciola hepatica, gel filtration on sephadex G-200, DEAE- Cellulose chromatography
