Effect of selected alcohol dehydrogenase inhibitors on human hepatic lactate dehydrogenase activity — an in vitro study
✍ Scribed by Jaroslaw Dudka; Franciszek Burdan; Justyna Szumilo; Edyta Tokarska; Agnieszka Korobowicz; Robert Klepacz; Renata Gieroba; Barbara Madej; Elzbieta Korobowicz
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 102 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0260-437X
- DOI
- 10.1002/jat.1094
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✦ Synopsis
Metabolic acidosis severely complicates methanol and ethylene glycol intoxications. Acidosis is caused by acid metabolites and can be intensified by lactate elevation. Lactate concentration depends on the NADH 2 /NAD ratio. Lactate dehydrogenase (LDH, E.C.1.1.1.27.) supplies more lactate when the level of NADH 2 is elevated. The aim of the study was to evaluate the effect of alcohol dehydrogenase (ADH) inhibitors and substrates: cimetidine, EDTA, 4methylpyrazole (4-MP), Ukrain and ethanol on LDH activity. The activity of LDH was determined spectrophotometrically in human liver homogenates incubated with cimetidine, EDTA, 4-MP and Ukrain at concentrations of 2 × × × × × 10