Gaudet S J, Razavi P, Caiafa G J, Chader G J
Laboratory of Retinal Cell and Molecular Biology, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Curr Eye Res. 1995 Oct;14(10):873-7. doi: 10.3109/02713689508995126.
Arylamine N-acetyltransferase (NAT) activity was identified and partially characterized in the bovine lens. According to size-exclusion HPLC, the molecular mass of the arylamine NAT is approximately 30-kDa. Based upon substrate specificity analysis, it is best described as an arylamine NAT which has some ability to N-acetylate arylalkylamines. This arylamine NAT acetylates para-aminobenzoic acid thereby demonstrating a monomorphic pattern of N-acetylation. It demonstrates low sensitivity to methotrexate inhibition as indicated by the relatively high IC50 value (470 microM). NAT could be involved in lenticular detoxification of both endogenous amines and exogenous drugs.
在牛晶状体中鉴定出芳胺N - 乙酰基转移酶（NAT）活性，并对其进行了部分表征。根据尺寸排阻高效液相色谱法，芳胺NAT的分子量约为30 kDa。基于底物特异性分析，它最适合被描述为一种芳胺NAT，具有一定的N - 乙酰化芳烷基胺的能力。这种芳胺NAT可使对氨基苯甲酸乙酰化，从而显示出N - 乙酰化的单态模式。如相对较高的IC50值（470 μM）所示，它对甲氨蝶呤抑制的敏感性较低。NAT可能参与晶状体对内源性胺类和外源性药物的解毒作用。
