Title of article :
Mechanism of biochemical action of substituted 4-methylbenzopyran-2-ones. Part 10: identification of inhibitors for the liver microsomal acetoxycoumarin: protein transacetylase Original Research Article
Author/Authors :
Hanumantharao G. Raj، نويسنده , , Ishwar Singh، نويسنده , , Ekta Kohli، نويسنده , , Ranju Kumari، نويسنده , , Garima Gupta، نويسنده , , Yogesh K Tyagi، نويسنده , , Ajit Kumar، نويسنده , , Ashok K. Prasad، نويسنده , , Narendra K. Kaushik، نويسنده , , Carl E Olsen، نويسنده , , Arthur C Watterson، نويسنده , , Virinder S. Parmar، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2003
Pages :
5
From page :
1015
To page :
1019
Abstract :
The quantitative structure–activity relationship (QSAR) studies conducted by us earlier revealed the cardinal role of the pyran ring carbonyl group in the acetoxy polyphenolic compounds for the acetoxy polyphenol:protein transacetylase (TAase) activity. Hence, an attempt was made to examine whether such substrate analogues of benzopyran acetates which lack in the pyran ring carbonyl group, such as 7-acetoxy-2,3-dihydro-2,2-dimethylbenzopyran (BPA), cetachin pentaacetate (CPA) and hematoxylin pentaacetate (HPA) could inhibit the 7,8-diacetoxy-4-methylcoumarin (DAMC):protein (glutathione-S-transferase) transacetylase activity. These compounds were indeed found to remarkably inhibit the TAase activity in a concentration dependent manner and exerted their inhibitory action very rapidly. Further BPA, CPA and HPA were found to abolish the TAase mediated activation of NADPH cytochrome C reductase as well as the inhibition of liver microsome catalyzed aflatoxin B1 (AFB1)-DNA binding by DAMC very effectively. These results strongly suggest that the acetoxybenzopyrans merit as potent inhibitors of TAase.
Journal title :
Bioorganic and Medicinal Chemistry
Serial Year :
2003
Journal title :
Bioorganic and Medicinal Chemistry
Record number :
1302592
Link To Document :
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