1. α-Chymotrypsin inhibition studies on the lignans from Vitex negundo Linn
- Author
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Muhammad Arif Lodhi, null Azhar-ul-Haq, M. Iqbal Choudhary, Abdul Malik, and Saeed Ahmad
- Subjects
Pharmacology ,chemistry.chemical_classification ,Proteases ,Vitex negundo ,biology ,Traditional medicine ,Chemistry ,General Medicine ,Alpha-chymotrypsin ,biology.organism_classification ,Serine ,Thrombin ,Enzyme ,Biochemistry ,Prolyl endopeptidase ,Drug Discovery ,medicine ,medicine.drug - Abstract
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.
- Published
- 2008
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