lignans has been researched along with alpha-chymotrypsin* in 3 studies
3 other study(ies) available for lignans and alpha-chymotrypsin
| Article | Year |
|---|---|
Urease inhibitory constituents from Daphne retusa.
The bioassay-guided fractionation of Daphne retusa Hemsl. has led to the isolation of a new aryl tetrahydronaphthalene lignan derivative named as daphnretusic acid (1), along with six new source compounds such as 5,7-dihydroxyflavone (2), 7-hydroxyflavone (3), 6-methoxyflavone (4), (+) pinoresinol (5), (+) sesamin (6), and β-sitosterol-3-O-β-D-glucopyranoside (7). Their structures were elucidated by (1)H NMR, (13)C NMR, 1D, 2D NMR, UV, IR, and EIMS analyses. All the fractions (n-hexane, CHCl3, AcOEt, CH3OH, and water) and pure compounds (1-7) were subjected to the assay of urease and α-chymotrypsin inhibitory activities. Chloroform and methanol soluble fractions showed moderate urease inhibition. Compound 2 exhibited significant urease inhibition with IC50 value 60.4 ± 0.72 μM, whereas compounds 1 and 3-7 remained inactive during urease inhibition and α-chymotrypsin bioassays. Topics: Chymotrypsin; Daphne; Flavonoids; Glucosides; Lignans; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Pakistan; Sitosterols; Tetrahydronaphthalenes; Urease | 2014 |
Kinetics studies on the lignan class of natural compounds that inhibits alpha-chymotrypsin.
The mechanism of inhibition of the alpha-chymotrypsin enzyme by two lignans of the fused bistetrahydrofuran series, epiexcelsin (1) and 5'-demethoxyepiexcelsin (2), which were isolated from the Commiphora mukul Engl., was investigated. Lineweaver-Burk and Dixon plots and their secondary replots showed that these compounds were noncompetitive inhibitors of the enzyme. K(i) values for 1 and 2 were found to be 22.29 +/- 0.015 and 336.30 +/- 0.053 microM, respectively. Topics: Chymotrypsin; Lignans; Magnoliaceae; Mathematics; Molecular Structure; Pakistan; Plants, Medicinal | 2009 |
alpha-Chymotrypsin inhibition studies on the lignans from Vitex negundo Linn.
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. Topics: Chymotrypsin; Lignans; Plants, Medicinal; Prolyl Oligopeptidases; Serine Endopeptidases; Serine Proteinase Inhibitors; Thrombin; Vitex | 2008 |