Lerner P, Nosé P, Ames M M, Lovenberg W
Neurochem Res. 1978 Oct;3(5):641-51. doi: 10.1007/BF00963765.
A modification of the tyrosine hydroxylase assay is described in which ascorbate, rather than 2-mercaptoethanol or dihydropteridine reductase with NADPH, is used as the reductant. Enzyme activity is 3-4 times higher with ascorbate than with the other reducing agents. Low blanks are obtained with the ascorbate system provided that catalase is also included. The tissue distribution and kinetic activation of the enzyme have been studied with the ascorbate assay. The results obtained are consistent with the biological and regulatory properties of the enzyme which have been determined with the other reducing systems.
本文描述了酪氨酸羟化酶测定法的一种改进方法,其中使用抗坏血酸而非2-巯基乙醇或与NADPH的二氢蝶啶还原酶作为还原剂。与其他还原剂相比,抗坏血酸存在时酶活性高3至4倍。如果也加入过氧化氢酶,则抗坏血酸系统的空白值较低。已使用抗坏血酸测定法研究了该酶的组织分布和动力学激活情况。获得的结果与用其他还原系统测定的该酶的生物学和调节特性一致。