Spectrophotometric method for determination of inorganic phosphate liberated in hydrolysis of ATP catalyzed by ATPase was modified in order to obtain faster procedure, which could also be used in none laboratory conditions. The modification has some advantages compared to the most used Pennial method: a) the reagents are stable for several months; b) the 45 min procedure of phosphomolibdate extraction by isobutanole-benzene is ommited, and the method is not dangerous for the analyst; c) color develops after 20 min. The method was tested on the determination of inorganic phosphate in the presence of cadmium nitrate as inhibitor of ATPase activity. The results were compared to the results obtained by Pennial method. The results obtained have shown some good agreements.

In our earlier work, we have shown that enzymes from rat brain synaptosomal membranes, Na(+)/K(+)-ATPase and Mg(2+)-ATPase, are promising biological components of a biosensor for lead detection. In this work, we represent our results of investigation with the same enzymes as biological components for the biosensor in presence of Hg(2+) ions in water. It was established that IC50 for Na(+)/K(+)-ATPase and Mg(2+)-ATPase is 6.9 and 5.5 x 10E-6 M, and the percentages of inhibition are 96% and 77% respectively. We concluded that these enzymes could be the base for developing biosensors for the presence of Hg(2+) ion in water. Since these enzymes maintain a stable activity for a longer period of time, they could be appropriate as components of biosensors for monitoring water quality.