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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。
丙氨酸氨基转移酶（ALT），旧称谷丙转氨酶（GPT），EC 2.6.1.2，广泛存在于动植物、微生物及培养细胞中，催化氨基酸与酮酸之间的转氨基反应，在氨基酸代谢中具有重要作用。本试剂盒采用2,4-二硝基苯肼（DNPH）比色法测定ALT活性：ALT催化丙氨酸与α-酮戊二酸发生转氨基反应，生成丙酮酸和谷氨酸；反应体系中加入2,4-二硝基苯肼溶液，既可终止酶促反应，又可与丙酮酸缩合生成丙酮酸-2,4-二硝基苯腙，在碱性条件下呈棕红色，该产物在520 nm处具有特征吸收峰。通过测定该波长下吸光值的增幅，即可精准计算样品中ALT的酶活力大小。
Alanine aminotransferase (ALT), formerly known as glutamic-pyruvic transaminase (GPT), EC 2.6.1.2, is widely present in animals, plants, microorganisms, and cultured cells. It catalyzes the transamination reaction between amino acids and keto acids, playing an important role in amino acid metabolism. This kit employs a 2,4-dinitrophenylhydrazine (DNPH) colorimetric method for the determination of ALT activity: ALT catalyzes the transamination of alanine with α-ketoglutarate to generate pyruvate and glutamate. The addition of 2,4-dinitrophenylhydrazine solution to the reaction system both terminates the enzymatic reaction and condenses with pyruvate to form pyruvate-2,4-dinitrophenylhydrazone, which appears brownish-red under alkaline conditions and exhibits a characteristic absorbance peak at 520 nm. By measuring the increase in absorbance at this wavelength, the ALT enzyme activity in the sample can be precisely calculated.
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