We have located links that may give you full text access.
Lactate-stimulated ethanol oxidation: Revisiting an old hypothesis.
Biochemical Pharmacology 2019 April 12
Liver slices from starved rats and incubated without other substrates oxidized ethanol at a rate of 4.1 µmols • h-1 • g-1 . Addition of 10 mmols • L-1 lactate increased this rate 2-fold. 4-methylpyrazole (4-MP), an alcohol dehydrogenase (ADH) inhibitor, drastically decreased the rate of ethanol oxidation, but did not inhibit the stimulation due to lactate. In the same context, liver acetaldehyde production, as the main by-product of ethanol oxidation, appeared to be much less inhibited by 4-MP in the presence of lactate. Aminotriazole (a catalase inhibitor), however, completely inhibited the stimulation. Furthermore, 2-hydroxybut-3-ynoate, an alpha-hydroxy acid oxidase inhibitor, completely abolished the stimulated ethanol oxidation promoted by lactate. Moreover, to determine the origin of the H2 O2 produced, we did liver subcellular fractionation and then analyzed their content in peroxisomes, mitochondria and catalase. We observed that cytoplasm and peroxisomes appears to be the main producers of H2 O2 , and that the acceleration of ethanol oxidation by lactate is completely dependent on catalase. In conclusion, the H2 O2 necessary to boost the catalase-dependent oxidation of ethanol appears to come from cytoplasm and peroxisomes, and is produced by the enzyme lactate oxidase.
Full text links
Related Resources
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app