作者: Neville J. Butcher , Kenneth F. Ilett , Rodney F. Minchin
DOI: 10.1124/MOL.57.3.468
关键词: Enzyme 、 Lactate dehydrogenase 、 Peripheral blood 、 Acetylation 、 Biology 、 Arylamine N-Acetyltransferase 1 、 Molecular biology 、 Biochemistry 、 Substrate (chemistry) 、 Peripheral blood mononuclear cell 、 EC50
摘要: Arylamine N-acetyltransferase-1 (NAT1) is a polymorphically expressed enzyme that widely distributed throughout the body. In present study, we provide evidence for substrate-dependent regulation of this enzyme. Human peripheral blood mononuclear cells cultured in medium supplemented withp-aminobenzoic acid (PABA; 6 μM) 24 h showed significant decrease (50–80%) NAT1 activity. The loss activity was concentration-dependent (EC50 ∼ 2 and selective because PABA had no effect on constitutively lactate dehydrogenase or aspartate aminotransferase. also induced down-regulation several human cell lines grown at confluence. Substrate-dependent not restricted to PABA. Addition other substrates, such as p-aminosalicylic acid, ethyl-p-aminobenzoate, p-aminophenol culture resulted (P