A spectrophotometric rate assay of aminoacylase.
作者： Hong-Yon Cho , Katsuyuki Tanizawa , Hidehiko Tanaka , Kenji Soda
DOI: 10.1016/0003-2697(87)90212-0
关键词: Chromatography 、 Alanine dehydrogenase 、 Chemistry 、 Biochemistry 、 Lactate dehydrogenase 、 Amino acid 、 Ninhydrin 、 Enzyme 、 Substrate (chemistry) 、 Aminoacylase 、 Thiol
摘要: Acetamidoacrylate, a synthetic N-acetyl unsaturated amino acid, was hydrolyzed to acetate, ammonia, and pyruvate by hog kidney, fungal, bacterial aminoacylases. A spectrophotometric procedure for rate assay of aminoacylase has been established with this substrate on the basis simultaneous reduction NADH alanine dehydrogenase. This is linear time enzyme concentration useful kinetic studies aminoacylase. not influenced significantly thiol compounds metal ions, which interfere ninhydrin methods traditionally used. Alanine dehydrogenase can be replaced lactate in reaction system.
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