Miller H K, Balis M E
Biochim Biophys Acta. 1977 Feb 3;474(3):435-44. doi: 10.1016/0005-2787(77)90272-6.
A Lineweaver-Burk analysis of a kinetic study of tRNA methylation by a 30-50% (NH4)2SO4 fraction from a weanling rat liver extract showed competitive inhibition with a Km for S-adenosylmethionine = 0.66 - 10(-6) M and a Ki for 3,4-dihydroxyphenylethylamine (dopamine) = 4 - 10(-5) M. The dopamine-inhibited methylation of tRNA appears to be linear with time. Rapid-flow dialysis studies indicated a S-adenosylmethionine binding constant of 0.65 - 10(-6) M. Dopamine appeared to interfere with the binding of S-adenosylmethionine to the weanling rat liver protein preparation but did not affect the binding of S-adenosylmethionine to protein in several systems in which dopamine did not inhibit tRNA methylase activity.
对来自断奶大鼠肝脏提取物的30 - 50%硫酸铵分级分离物进行的tRNA甲基化动力学研究的Lineweaver - Burk分析表明,存在竞争性抑制,其中S - 腺苷甲硫氨酸的Km = 0.66×10⁻⁶ M,3,4 - 二羟基苯乙胺(多巴胺)的Ki = 4×10⁻⁵ M。多巴胺抑制的tRNA甲基化似乎与时间呈线性关系。快速流动透析研究表明S - 腺苷甲硫氨酸结合常数为0.65×10⁻⁶ M。多巴胺似乎干扰了S - 腺苷甲硫氨酸与断奶大鼠肝脏蛋白质制剂的结合,但在多巴胺不抑制tRNA甲基ase活性的几个系统中,并不影响S - 腺苷甲硫氨酸与蛋白质的结合。