Watanabe T, Kambe H, Imamura I, Taguchi Y, Tamura T, Wada H
Anal Biochem. 1983 Apr 15;130(2):321-7. doi: 10.1016/0003-2697(83)90594-8.
A method for enzymatic assay of imidazole acetic acid (ImAA) was developed, based on the strict substrate specificity of imidazole acetate monooxygenase from Pseudomonas sp. [Maki et al. (1969) J. Biol. Chem., 244., 2942-2950], which catalyzes concomitant conversion of NADH to NAD+. Thus, ImAA was determined by measuring decrease in absorbancy at 340 nm. Tissue extracts were partially purified and/or concentrated by column chromatography on Bio-Rad AG-1 before enzymatic assay. The lowest measurable level of ImAA by this method was 2 nmol.
基于来自假单胞菌属的咪唑乙酸单加氧酶严格的底物特异性[牧木等人（1969年）《生物化学杂志》，第244卷，2942 - 2950页]，开发了一种用于酶促测定咪唑乙酸（ImAA）的方法，该酶催化NADH同时转化为NAD⁺。因此，通过测量340 nm处吸光度的降低来测定ImAA。在酶促测定之前，组织提取物通过在Bio - Rad AG - 1上进行柱色谱法进行部分纯化和/或浓缩。用这种方法可测量的ImAA的最低水平为2 nmol。
