Tran V T, Snyder S H
J Biol Chem. 1981 Jan 25;256(2):680-6.
Histidine decarboxylase from fetal rat liver was purified to near-homogeneity. The purified enzyme has a molecular weight of 210,000, and appears to contain two subunits with molecular weights of 145,000 and 66,000, respectively. The enzyme is inhibited by heavy metals such as Hg2+ and Zn2+ and sulfhydryl-reactive compounds such as 5,5'-dithiobis-2-nitrobenzoic acid. The enzyme is partially dependent on exogenous pyridoxal phosphate. Extensive dialysis results in 50% loss of enzyme activity which can be fully recovered by adding pyridoxal phosphate. Affinity of pyridoxal phosphate for the apoenzyme is 0.1 microM at pH 6.8. Antibody against purified histidine decarboxylase was raised in rabbits. The antibody has been employed in immunohistochemical studies to visualize histidine decarboxylase containing cells and neuronal processes in rat stomach and brain, respectively. Immunologic studies indicate that histidine decarboxylase from brain, gastric mucosa, and fetal rat liver share common antigenic properties.
来自胎鼠肝脏的组氨酸脱羧酶被纯化至接近均一。纯化后的酶分子量为210,000，似乎包含分别为145,000和66,000的两个亚基。该酶被重金属如Hg2+和Zn2+以及巯基反应性化合物如5,5'-二硫代双-2-硝基苯甲酸抑制。该酶部分依赖于外源性磷酸吡哆醛。广泛透析导致酶活性丧失50%，通过添加磷酸吡哆醛可完全恢复。在pH 6.8时，磷酸吡哆醛对脱辅基酶的亲和力为0.1 microM。用纯化的组氨酸脱羧酶对兔进行免疫。该抗体已用于免疫组织化学研究，分别在大鼠胃和脑中观察含组氨酸脱羧酶的细胞和神经突起。免疫学研究表明，来自脑、胃黏膜和胎鼠肝脏的组氨酸脱羧酶具有共同的抗原特性。
