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  • 1 Department of General Biophysics, University of Lodz 12/16 Banacha St., 90-237 Lodz, Poland
  • | 2 Department of General Biophysics, University of Lodz 12/16 Banacha St., 90-237 Lodz, Poland
  • | 3 Department of General Biophysics, University of Lodz 12/16 Banacha St., 90-237 Lodz, Poland
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AMP-deaminase (EC 3.5.4.6) is an enzyme responsible for stabilising adenylate energy changes. The properties of this enzyme are controlled by various ligands of hydrophobic nature. An investigation of enzyme activity alterations under the influence of natural phenolic acids (tannic, ellagic and gallic) which are soluble in water, could evidence the biological toxicity of these compounds. In our study purified AMP-deaminase isolated from white muscle of Cyprinus carpiowas exposed to phenolic acids in the concentration range of 1 to 50 µM as well as to tannic acid in the presence of Cu2+ions (5 µM). On the basis of the obtained results we can conclude that among the tested acids, gallic acid did not contribute to the change in AMP-deaminase activity, whereas ellagic acid diminished its activity at the highest concentration (50 µM). Tannic acid caused a significant decrease in the enzyme activity in comparison to control for all used concentrations. Cu2+ions alone reduced the activity of AMP-deaminase for all studied concentrations. A combined action of a chosen Cu2+ions concentration (5 µM) with tannic acid at the concentration higher than 2 µM resulted in a decrease in the enzyme activity, but for lower tannic acid concentration of 1 µM the activity of AMP-deaminase was stimulated. These experiments showed that tannic acid may stop free radical chain reactions only at low concentrations (1 µM) in the presence of Cu2+ions (5 µM).

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