Comparative sensitivities of in vitro acetylcholinesterase inhibition by novel
IR@IICT: CSIR-Indian Institute of Chemical Technology, Hyderabad
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Creator |
Rahman, M.F
Mahboob, M Grover, P |
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Date |
2008-12-15T11:27:37Z
2008-12-15T11:27:37Z 2004 |
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Identifier |
http://hdl.handle.net/123456789/55
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Description |
In the present investigation, in vitro effect of RPR-II and RPR-V, two novel phosphorothionates were compared with
monocrotophos (MCP) in RBCs, brain and liver of broiler chicken (Callus gallus) with special reference to acetylcholinesterase
(AChE). The purpose of the study was to quantify "in vitro" by means of the 50 percent inhibition (IC,,) using novel
organophosphorus compounds as inhibitors. Cholinesterase activities with acetylthiocholine iodide as substrate in different
tissues of chicken were measured photometrically in the presence of different concentrations of pesticides. As the concentration
of the pesticides increased, the inhibition was also induced in a linear pattern. The IC50, observed for RBC AChE was 1.92
mM by MCP, whereas the inhibition was greater than 20 mM in case of RPR-II and RPR-V. In case of brain AChE, the
IC50, obtained was 1.21,5.76 and 0.97 mM for RPR-II, RPR-V and MCP, respectively. Similarly, with regard to liver AChE
the IC50, observed were 7.69, 8.63 and 0.18 mM for RPR-II, RPR-V and MCP, respectively. Besides, MCP was found to be
48 times more potent inhibitor than RPR-V. The kinetic constants (Vmax and Km) showed a decrease with all the three
compounds in RBCs, brain and liver of chicken, indicating non-competitive inhibition. The current study suggests that RPRII
and RPR-V having P=S moiety in their structure are less neurotoxic than MCP, which has a P=O moiety in its structure.
From the present study, it can be concluded that the in vitro AChE assay is a sensitive assay and can be used as biochemical
marker for the exposure of organophosphorus compounds.
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Subject |
Organophosphorus compounds
In vitro acetylcholinesterase Chicken |
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Title |
Comparative sensitivities of in vitro acetylcholinesterase inhibition by novel
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Type |
Article
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