Rougraff P M, Paxton R
Comp Biochem Physiol B. 1987;86(3):601-6. doi: 10.1016/0305-0491(87)90455-x.
Arylamine acetyltransferase (EC 2.3.1.5) was purified 120-fold from chicken liver. The enzyme showed a rise in activity from pH 6.5 to 7.7 followed by a constant activity to about pH 8.6. The relative molecular weight of the enzyme was about 34,000. The apparent Km for acetyl-CoA was 13 microM with 4-nitroaniline as acetyl-acceptor. CoA was a noncompetitive inhibitor relative to acetyl-CoA with apparent Ki value of 110 microM. With 4-methylaniline as substrate, arylamine acetyltransferase activity in pigeon liver was about 8 times greater than in chicken liver, and about 40 times greater than in rabbit.
从鸡肝中纯化出了芳胺乙酰转移酶（EC 2.3.1.5），纯化倍数为120倍。该酶的活性在pH 6.5至7.7之间上升，然后在约pH 8.6之前保持恒定。该酶的相对分子质量约为34,000。以4-硝基苯胺作为乙酰受体时，乙酰辅酶A的表观Km为13微摩尔。相对于乙酰辅酶A，辅酶A是一种非竞争性抑制剂，表观Ki值为110微摩尔。以4-甲基苯胺为底物时，鸽肝中的芳胺乙酰转移酶活性比鸡肝中的高约8倍，比兔肝中的高约40倍。
