Gaudet S J, Chader G J
Laboratory of Retinal Cell and Molecular Biology, National Eye Institute, National Institutes of Health, Bethesda, MD 20892.
Curr Eye Res. 1992 Dec;11(12):1185-92. doi: 10.3109/02713689208999543.
Arylamine N-acetyltransferase (NAT) activity was partially purified and characterized in bovine retina. Upon examining the retinal supernatant for multiple ionic species, only one NAT activity was detected. Based upon its substrate specificity, it is best described as an arylamine NAT. According to size-exclusion HPLC, the molecular mass of the arylamine NAT is approximately 30-kDa. This arylamine NAT acetylates p-aminobenzoic acid thereby demonstrating a monomorphic pattern of acetylation. The NAT activity demonstrated low sensitivity to methotrexate inhibition as indicated by a high IC50 value (480 microM).
在牛视网膜中对芳胺N - 乙酰基转移酶（NAT）活性进行了部分纯化和表征。在检测视网膜上清液中的多种离子成分时，仅检测到一种NAT活性。根据其底物特异性，它最适合被描述为芳胺NAT。根据尺寸排阻高效液相色谱法，芳胺NAT的分子量约为30 kDa。这种芳胺NAT使对氨基苯甲酸乙酰化，从而显示出单态乙酰化模式。如高IC50值（480 μM）所示，NAT活性对甲氨蝶呤抑制表现出低敏感性。
