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Effects of some metals on paraoxonase activity from shark Scyliorhinus canicula
Demet Sayın1, Dilek Türker Cakır, Nahit Gençer
1Department of Chemistry, Science and Art Faculty, Cagis Yerleskesi, Balikesir University, Balikesir, Turkey.
Abstract:
Paraoxonase (PON) is an organophosphate hydrolyser enzyme which also has antioxidant properties in metabolism. Due to its crucial functions, the inhibition of the enzyme is undesirable and very dangerous. PON enzyme activity should not be altered in any case. Inhibitory investigations of this enzyme are therefore important and useful. Metal toxicology of enzymes has become popular in the recent years. Here, we report the in vitro inhibitory effects of some metal ions, including Ni(2+), Cd(2+), Cu(2+) and Hg(2+), on the activity of shark serum PON (SPON). For this purpose, we first purified the enzyme from shark Scyliorhinus canicula (LINNAEUS, 1758) serum and analysed the alterations in the enzyme activity in the presence of metal ions. The K(M) and V(max) is 0.227 mM and 454.545 U/mL, respectively. The results show that metal ions exhibit inhibitory effects on SPON1 at low concentrations with IC(50) values ranging from 0.29 to 2.00 mM. Copper was determined to be the most effective inhibitor with IC(50) of 0.29 mM.
Insights
Investigating metal ion toxicity, this study found that nickel, cadmium, copper, and mercury ions inhibit shark serum paraoxonase (SPON) enzyme activity. Copper ions were the most potent inhibitors, highlighting risks associated with heavy metal exposure.
Area of Science:
- Biochemistry
- Enzymology
- Environmental Toxicology
Background:
- Paraoxonase (PON) is a vital enzyme with organophosphate hydrolyzing and antioxidant functions.
- Enzyme activity is crucial and should not be altered; inhibition can be dangerous.
- Metal ion toxicology on enzymes is an emerging area of research.
Purpose of the Study:
- To investigate the in vitro inhibitory effects of specific metal ions on shark serum paraoxonase (SPON) activity.
- To determine the inhibitory potential of Ni(2+), Cd(2+), Cu(2+), and Hg(2+) on SPON.
Main Methods:
- Purification of shark serum paraoxonase (SPON) from Scyliorhinus canicula serum.
- Analysis of SPON activity in the presence of varying concentrations of metal ions (Ni2+, Cd2+, Cu2+, Hg2+).
- Determination of enzyme kinetics (K(M), V(max)) and inhibitory parameters (IC(50)).
Main Results:
- All tested metal ions (Ni2+, Cd2+, Cu2+, Hg2+) demonstrated inhibitory effects on SPON activity at low concentrations.
- The IC(50) values for the metal ions ranged from 0.29 to 2.00 mM.
- Copper (Cu2+) exhibited the strongest inhibitory effect, with an IC(50) of 0.29 mM.
Conclusions:
- Metal ions, particularly copper, can significantly inhibit shark serum paraoxonase activity in vitro.
- These findings underscore the potential toxicological impact of heavy metals on essential enzyme functions.
- Further research into metal-enzyme interactions is warranted to understand broader physiological implications.
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