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Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Alcohol dehydrogenase (ADH), systematically named as alcohol: NAD⁺ oxidoreductase, is abundantly present in the livers of humans and animals, as well as in plant and microbial cells. It is a zinc-containing metalloenzyme with broad substrate specificity. Alcohol dehydrogenase 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, alcohol dehydrogenase and aldehyde dehydrogenase (ALDH) together form the alcohol dehydrogenase system, which is involved in ethanol metabolism within the body. As a key enzyme for short-chain alcohol metabolism in living organisms, ADH plays a crucial role in many physiological processes. Pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH) are key enzymes in the ethanol fermentation pathway. The accumulation of metabolic products in anaerobic respiration pathways can be toxic to cells, affecting mitochondrial structure and the activity of enzymes related to the tricarboxylic acid cycle. The detection principle of this kit is based on the reduction of acetaldehyde to ethanol by NADH under weakly alkaline conditions, catalyzed by ADH. For every molecule of acetaldehyde catalyzed by ADH, one molecule of NADH is consumed. The consumption rate of NADH is determined by spectrophotometry (using a spectrophotometer) to measure changes in absorbance at 340 nm. This allows for the calculation of alcohol dehydrogenase activity levels. This kit is primarily used to detect alcohol dehydrogenase activity in plant samples, serum, and other biological materials. This product is intended for research use only and is not suitable for clinical diagnosis or other purposes.
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