α-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 α-chymotrypsin, thrombin and prolyl endopeptidase. Compounds 3 and 4 were found to be active only against α-chymotrypsin and were noncompetitive and competitive inhibitors of the enzyme, respe...
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Published in | Journal of enzyme inhibition and medicinal chemistry Vol. 23; no. 3; pp. 400 - 405 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
England
Informa UK Ltd
01.06.2008
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Subjects | |
Online Access | Get full text |
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Summary: | The lignans (1-8) isolated from the roots of Vitex negundo Linn. were screened against the serine proteases α-chymotrypsin, thrombin and prolyl endopeptidase. Compounds 3 and 4 were found to be active only against α-chymotrypsin and were noncompetitive and competitive inhibitors of the enzyme, respectively. Ki values were found to be in the range 31.75-47.11 μM. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1475-6366 1475-6374 |
DOI: | 10.1080/14756360701584653 |