تأثير المثبطات اليوريز المنقى من البكتريا المتقلبات Proteus vulgaris المعزولة محليا

الملخص EN

Examination the urease activity which purified from Proteus vulgaris in the presence of six inhibitors were thiourea, hydroxy urea, EDTA, ß-Mercaptoethanol, flurofamide and Para - Benzoquinon has been observed that all these compounds had been urease inhibitors, results showed that all of them where competitive inhibitors except p- benzoqinon non-competitive.

The mechanism inhibition were studying of all inhibitors compounds, there ß-Mercaptoethanol has regained enzyme effectively with the p - benzoquinon, which indicates the existence of a sulfhydryl group (SH) on-site effective in not affected by the act of each thiourea and hydroxurea and the EDTA, either when using ions nickel, all inhibitors may affected by their work, except ß -mercaptoethanol and p-benzoqinon and not recovery the enzyme activity, which indicates that the binding site inhibitors is effective, and the results of the current study appeared that the inhibitor flurofamide was the most effective inhibitors of the urease.