Previous studies clearly indicated that membrane enzymes - ATPases i.e. Na, K-ATPase and Mg-ATPase, responded to presence of various organic and inorganic pollutants. In this work effect of mercury and cadmium on these enzymes activities was investigated in synaptic plasma membranes partially immobilized on microliter plate. Comparing those activities with the control enzyme activities obtained with native and partially immobilized mambranes it was concluded that: a. both metals exerted a concentration-dependent inhibition of investigated enzymes, b. for partially immobilized membranes estimated half maximum inhibition (IC50) values for Na, K-ATPase were IC50 (Hg) = 0.9 micromol/cubic cm, IC50 (cd) = 35 micromol/cubic cm and for Mg - ATPase IC50 (Hg) = 3.5 micromol/cubic cm, IC50 (Cd) = 36 micromol/cubic cm; for native membranes IC50 for Na,K-ATPase were IC50 (Hg) =3.3 micromol/cubic cm, IC50 (Cd) = 2 micromol/cubic cm and for Mg ATPase IC50 (Hg) = 2.3 micromol/cubic cm, IC50 (Cd) = 0.2 mmol/cubic cm. Obtained results indicate avaibility of microtitar plates for partially immobilization of membranes with aim to form a new biosensor for heavy metals detection.

The reaction of Pd(II) with 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalen-3,6-disulphonic acid immobilized by physical sorption onto Dowex 1-X8 ion-exchange resin was investigated with the aim to develop the sorption-spectroscopic test method for the detection of low Pd(II) concentrations in water. The resin phase absorption spectra of the reagent and its Pd(II) complex were followed. The immobilized reagent has the spectral characteristics similar to those in the water and forms with Pd(II) 1:1 complex with the absorption maximum at 650 nm. Parameters, such as pH, wavelength and contact time have been optimized for a given amount of the sorbed reagent. The experimental conditions for the linear dependence of absorbance vs. Pd(II) concentration have been determined.