Please use this identifier to cite or link to this item:
Full metadata record
|dc.identifier.citation||Biologia. Vol.67, No.4 (2012), 762-766||en_US|
|dc.description.abstract||Cholinesterase (ChE) was characterized in whole bodies of adult riceland prawns, Macrobrachium lanchesteri, based on substrate preference and inhibitor sensitivity. M. lanchesteri ChE activity was mainly attributable to acetylcholinesterase (AChE) since it preferentially hydrolyzed an AChE-specific substrate, acetylthiocholine iodide, over s-butyrylthiocholine iodide and was sensitive to 1,5-bis-(4-allyldimethyl-ammoniumphenyl)-pentan-3-one dibromide, a specific inhibitor for AChE. The effect of chlorpyrifos exposure on M. lanchesteri were also investigated. The 24, 48, 72 and 96 h LC 50 values for chlorpyrifos were 3. 37, 2. 76, 2. 58 and 2. 53 μg L -1 , respectively. Based on these values, adult M. lanchesteri were exposed to 0. 5, 1. 5, 2. 5 and 3. 5 μg chlorpyrifos L -1 for 24, 48, 72 and 96 h. Chlorpyrifos appeared to induce drastic enzymatic responses in M. lanchesteri. AChE activity was inhibited after 24 h of exposure in a dose- and time-dependent manner. The levels of lipid peroxidation increased significantly after 24 h of exposure. However, the activities of the antioxidant enzyme, catalase, and the detoxification enzyme, glutathione S-transferase, were reduced. In conclusion, M. lanchesteri is sensitive to chlorpyrifos and can serve as a bioindicator species for freshwater environmental assessment. © 2012 Versita Warsaw and Springer-Verlag Wien.||en_US|
|dc.subject||Agricultural and Biological Sciences||en_US|
|dc.subject||Biochemistry, Genetics and Molecular Biology||en_US|
|dc.title||Enzymatic responses of the riceland prawn, Macrobrachium lanchesteri, to chlorpyrifos exposure||en_US|
|Appears in Collections:||Scopus 2011-2015|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.