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Enzyme Inhibition by Allicin, the Molluscicidal Agent of Allium sativum L. (Garlic)
Author(s) -
Singh V. K.,
Singh D. K.
Publication year - 1996
Publication title -
phytotherapy research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 129
eISSN - 1099-1573
pISSN - 0951-418X
DOI - 10.1002/(sici)1099-1573(199608)10:5<383::aid-ptr855>3.0.co;2-9
Subject(s) - allicin , alkaline phosphatase , acetylcholinesterase , biochemistry , enzyme , in vivo , uncompetitive inhibitor , biology , dehydrogenase , lactic dehydrogenase , succinate dehydrogenase , chemistry , pharmacology , non competitive inhibition , microbiology and biotechnology
Allicin, a molluscicidal component of garlic inhibited the activity of acetylcholinesterase, lactic dehydrogenase and alkaline phosphatase in in vivo and in vitro exposure against Lymnaea acuminata . It was observed that succinic dehydrogenase activity in the nervous tissue of Lymnaea acuminata was increased in in vivo treatment whereas with in vitro exposure, allicin caused no significant change in succinic dehydrogenase activity. The inhibition kinetics of these enzymes indicates that allicin caused an uncompetitive inhibition of AChE and a competitive inhibition of LDH and alkaline phosphatase.