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Cu2+-dependent hydrolysis of O-hexyl 2,5-dichlorophenyl phosphoramidate by reptile sera.
- Source :
-
Chemico-Biological Interactions . Sep2023, Vol. 382, pN.PAG-N.PAG. 1p. - Publication Year :
- 2023
-
Abstract
- This study shows the EDTA-resistant, Ca2+ and Cu2+-dependent hydrolysis of O-hexyl 2,5-dichlorophenyl phosphoramidate (HDCP) compound in reptiles sera determined by spectrophotometry UV/Vis and chiral chromatography. Samples of ten reptile species were incubated with aliquot of 100 or 400 μM HDCP in presence of 100 or 300 μM Cu2+, or 2.5 mM Ca2+ or 5 mM EDTA at 37 °C for 30–60 min. The results shown an activator effect of Cu2+ on HDCP hydrolysis in freshwater turtles sera (Trachemys scripta , Chelydra serpentina and Macrochelys temminckii) because the levels of 2,5-dichlorophenol (DCP; product hydrolysis) were similar (∼37 μM DCP) to chicken serum (positive control group). The marine turtles (Chelonia mydas and Eretmochelys imbricata) and crocodiles (Crocodylus acutus and Crocodylus moreletii) showed ∼50% less HDCPase activity (13–17 μM DCP) compared to the HDCPase activity of the freshwater turtle species. Terrestrial reptile species (snakes and lizards) showed around 25% of activity (7–13 μM DCP) with both copper concentrations. These Cu2+-dependent hydrolysis were stereospecific to R(+)-HDCP (p˂0.05) in the three freshwater turtle species that showed similar hydrolysis to the chicken serum. However, the Ca2+ did not show a significant activating effect on the HDCPase activity (1–8 μM DCP) in any reptile serum. Their hydrolysis levels were very similar to those of EDTA-resistant activity. The present study demonstrates a Cu2+-dependent A-esterase (HDCPase) activity in turtles and points serum albumin as the cuproprotein responsible for this activity, reinforcing its N-terminal sequence (DAEH) as a catalytic center. • Pesticides. • Hydrolysis. • Copper. • Reptiles. • Stereoselectivity. [ABSTRACT FROM AUTHOR]
- Subjects :
- *REPTILES
*TURTLES
*CROCODILES
*HAWKSBILL turtle
*HYDROLYSIS
*GREEN turtle
*VENOM
Subjects
Details
- Language :
- English
- ISSN :
- 00092797
- Volume :
- 382
- Database :
- Academic Search Index
- Journal :
- Chemico-Biological Interactions
- Publication Type :
- Academic Journal
- Accession number :
- 169948073
- Full Text :
- https://doi.org/10.1016/j.cbi.2023.110637