Abstract
The inhibition of ethoxy coumarin O-deethylase (ECOD) activity by aucubin and its aglycone was examined in a microsomal system and in freshly isolated hepatocytes. Aucubin was found to be inactive but the aglycone was found to be a potent time-dependent inhibitor of ECOD activity in both systems. The close structural similarity between the aglycone of aucubin and glutaraldehyde suggests a similar mechanism of enzyme inhibition through protein cross-linking by Schiff reactions. The similarity between the 2 compounds was demonstrated through their closely similar binding spectra to bovine serum albumin. The biological activities reported for the aglycone are suggested to be due to this similarity to glutaraldehyde.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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7-Alkoxycoumarin O-Dealkylase / antagonists & inhibitors*
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Animals
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Cattle
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Cross-Linking Reagents / chemistry
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Cross-Linking Reagents / metabolism
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Cross-Linking Reagents / pharmacology
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Cytochrome P-450 Enzyme Inhibitors*
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / metabolism
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Enzyme Inhibitors / pharmacology
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Glucosides / chemistry
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Glucosides / metabolism
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Glucosides / pharmacology*
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Glutaral / chemistry
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In Vitro Techniques
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Iridoid Glucosides
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Iridoids*
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L-Lactate Dehydrogenase / metabolism
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Male
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Microsomes, Liver / drug effects
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Microsomes, Liver / metabolism
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Molecular Structure
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Protein Binding
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Pyrans / chemistry
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Pyrans / metabolism
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Pyrans / pharmacology
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Rats
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Rats, Wistar
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Schiff Bases / chemistry
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Schiff Bases / metabolism
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Schiff Bases / pharmacology
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Serum Albumin, Bovine / metabolism
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Spectrophotometry, Ultraviolet
Substances
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Cross-Linking Reagents
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Cytochrome P-450 Enzyme Inhibitors
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Enzyme Inhibitors
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Glucosides
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Iridoid Glucosides
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Iridoids
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Pyrans
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Schiff Bases
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Serum Albumin, Bovine
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aucubin
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aucubigenin
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L-Lactate Dehydrogenase
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7-Alkoxycoumarin O-Dealkylase
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Glutaral