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Monoamine oxidase and succinate dehydrogenase inhibitory properties of substituted mercaptoquinazolones
Author(s) -
Mehrotra Suman,
Barthwal J. P.,
Saxena A. K.,
Bhargava K. P.,
Parmar S. S.
Publication year - 1981
Publication title -
journal of heterocyclic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.321
H-Index - 59
eISSN - 1943-5193
pISSN - 0022-152X
DOI - 10.1002/jhet.5570180619
Subject(s) - chemistry , succinate dehydrogenase , monoamine oxidase , anthranilic acid , inhibitory postsynaptic potential , in vitro , enzyme , stereochemistry , organic chemistry , biochemistry , neuroscience , biology
Twelve 6‐substituted‐2‐(1′‐mercaptoacetyl‐3′‐arylurea)‐3‐phenyl‐4‐quinazolones were synthesized by condensation of 6‐substituted anthranilic acids and aryl isothiocyanates followed by reaction with chloroacetyl arylurea. These compounds were characterized by their sharp melting points and elemental analyses. All compounds were evaluated for their enzyme inhibitory activity. It was found that all substituted quinazolones at a final concentration of 2 × 10 −4 M inhibited in vitro monoamine oxidase and succinate dehydrogenase activity of rat brain homogenates and the degree of inhibition ranged from 11–77% and 25–53%, respectively.