Abstract | BACKGROUND: METHODS: RESULTS: Our results showed that methocarbamol can inhibit sucrase activity and reduce the maximum reaction velocity (Vmax) of the enzyme by a non-competitive pattern. Measurement of IC50 and Ki of the drug revealed that methocarbamol did not bind the enzyme with high affinity. Fluorescence measurement showed that the drug binds to free enzyme and enzyme-substrate complexes that were accompanied by structural changes on the enzyme. Guaifenesin, which has a similar structure to methocarbamol, does not affect the activity of sucrase. CONCLUSIONS:
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Authors | Dariush Minai-Tehrani, Allaleh Masoudnia, Sana Alavi, Raheleh Osmani, Leila Lotfi, Mitra Asghari, Mahdi Pirsalehi, Zahra Sobhani-Damavandifar |
Journal | Drug metabolism and drug interactions
(Drug Metabol Drug Interact)
Vol. 27
Issue 4
Pg. 225-8
( 2012)
ISSN: 0792-5077 [Print] Germany |
PMID | 23023692
(Publication Type: Journal Article)
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Chemical References |
- Enzyme Inhibitors
- Methocarbamol
- Sucrase
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Topics |
- Enzyme Inhibitors
(pharmacology)
- Fluorescence
- Methocarbamol
(pharmacology)
- Sucrase
(antagonists & inhibitors)
- Yeasts
(enzymology)
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