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在色谱分析、有机合成和交叉偶联反应领域已被 0 篇同行评审文献引用。
乙醛脱氢酶(ALDH,EC 1.2.1.10)是醛脱氢酶家族的重要成员,广泛存在于动物、植物及微生物体内,主要催化乙醛氧化为乙酸,在酒精代谢中发挥关键作用。在人类及多数动物体内,线粒体乙醛脱氢酶能够将有毒的醛类转化为相应的酸,从而参与细胞解毒过程,因此该酶在毒理学、药物代谢及肝脏疾病研究中备受关注;同时,ALDH在分子生物学检测及酒精代谢相关疾病的诊断中也具有广泛的应用价值。本试剂盒的测定原理为:在辅酶Ⅰ(NAD⁺)存在下,ALDH催化乙醛和NAD⁺转化为乙酸和NADH;NADH在340 nm处具有特征吸收峰,而NAD⁺无此吸收,因此通过测定340 nm处吸光度的增加速率,即可定量计算ALDH的酶活性。
Aldehyde dehydrogenase (ALDH, EC 1.2.1.10) is an important member of the aldehyde dehydrogenase family, widely distributed in animals, plants, and microorganisms. It primarily catalyzes the oxidation of acetaldehyde to acetic acid, playing a critical role in alcohol metabolism. In humans and most animals, mitochondrial aldehyde dehydrogenase is capable of converting toxic aldehydes into their corresponding acids, thereby participating in cellular detoxification processes. Consequently, this enzyme has attracted considerable attention in toxicology, drug metabolism, and liver disease research. Meanwhile, ALDH also has broad application value in molecular biology assays and the diagnosis of alcohol metabolism‑related diseases. The assay principle of this kit is as follows: in the presence of coenzyme I (NAD⁺), ALDH catalyzes the conversion of acetaldehyde and NAD⁺ to acetic acid and NADH. NADH exhibits a characteristic absorption peak at 340 nm, whereas NAD⁺ does not. Therefore, the ALDH enzyme activity can be quantitatively calculated by measuring the rate of increase in absorbance at 340 nm.