Enzyme Inhibition by Molluscicidal Components ofMyristica fragransHoutt. in the Nervous Tissue of SnailLymnaea acuminata
Author(s) -
Preetee Jaiswal,
Pradeep Kumar,
VK Singh,
D. K. Singh
Publication year - 2009
Publication title -
enzyme research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.439
H-Index - 39
eISSN - 2090-0406
pISSN - 2090-0414
DOI - 10.4061/2010/478746
Subject(s) - myristica fragrans , snail , acetylcholinesterase , biology , non competitive inhibition , enzyme , biochemistry , aché , pharmacology , chemistry , botany , ecology
This study was designed to investigate the effects of molluscicidal components of Myristica fragrans Houtt. (Myristicaceae) on certain enzymes in the nervous tissue of freshwater snail Lymnaea acuminata Lamarck (Lymnaeidae). In vivo and in vitro treatments of trimyristin and myristicin (active molluscicidal components of Myristica fragrans Houtt.) significantly inhibited the acetylcholinesterase (AChE), acid and alkaline phosphatase (ACP/ALP) activities in the nervous tissue of Lymnaea acuminata . The inhibition kinetics of these enzymes indicates that both the trimyristin and myristicin caused competitive noncompetitive inhibition of AChE. Trimyristin caused uncompetitive and competitive/noncompetitive inhibitions of ACP and ALP, respectively whereas the myristicin caused competitive and uncompetitive inhibition of ACP and ALP, respectively. Thus results from the present study suggest that inhibition of AChE, ACP, and ALP by trimyristin and myristicin in the snail Lymnaea acuminata may be the cause of the molluscicidal activity of Myristica fragrans .
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