BioReagent BioReagent for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
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Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Alcohol Dehydrogenase (ADH), systematic name alcohol: NAD⁺ oxidoreductase, is a zinc-containing metalloenzyme with broad substrate specificity. It is abundantly present in the livers of humans and animals, as well as in plant and microbial cells. ADH utilizes nicotinamide adenine dinucleotide (NAD⁺) as a coenzyme to catalyze the reversible reaction between primary alcohols and aldehydes: CH₃CH₂OH + NAD⁺ → CH₃CHO + NADH + H⁺. In humans and mammals, ADH together with acetaldehyde dehydrogenase (ALDH) constitutes the alcohol dehydrogenase system, which is involved in ethanol metabolism and plays a vital role as a key metabolic enzyme. As a critical enzyme in the metabolism of short-chain alcohols, ADH is important in numerous physiological processes. Additionally, pyruvate decarboxylase (PDC) and ADH are key enzymes in the ethanol fermentation pathway. The accumulation of metabolites from anaerobic respiration can be toxic to cells, affecting mitochondrial structure and the activity of enzymes related to the tricarboxylic acid (TCA) cycle. Under weakly alkaline conditions, using acetaldehyde as the substrate, ADH catalyzes the reduction of acetaldehyde to ethanol by NADH. Each molecule of acetaldehyde reduced consumes one molecule of NADH. By measuring the change in absorbance at 340 nm using spectrophotometry (full-wavelength microplate reader), the rate of NADH consumption is determined, from which the activity level of alcohol dehydrogenase can be calculated. This kit is primarily used to detect alcohol dehydrogenase activity in samples such as plant tissues and serum. It is intended for research purposes only and is not suitable for clinical diagnosis or other applications.
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