Journal of Enzyme Inhibition and Medicinal Chemistry · 2008 · 20 citations · 11 references
Life SciencesBiochemistryPharmacologyDrug DiscoveryEnzymologyStructure-activity RelationshipsEnzyme InhibitionMedicinal PlantsProteolytic EnzymesPlant ProteasesProtease Inhibition
The lignans (1-8) isolated from the roots of Vitex negundo Linn. were screened against the serine proteases alpha-chymotrypsin, thrombin and prolyl endopeptidase. Compounds 3 and 4 were found to be active only against alpha-chymotrypsin and were noncompetitive and competitive inhibitors of the enzyme, respectively. Ki values were found to be in the range 31.75-47.11 microM.
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The determination of enzyme inhibitor constants
Martin Dixon · Biochemical Journal · 1953 · 4.1K citations · Full text