Semenenko F M, Cuello A C, Goldstein M, Lee K Y, Sidebottom E
J Histochem Cytochem. 1986 Jun;34(6):817-21. doi: 10.1177/34.6.2871071.
The catecholaminergic neurons of the nervous system have been studied histochemically with fluorescent derivatives of catecholamines and immunocytochemically using antibodies against their biosynthetic enzymes. The immunocytochemical techniques yield permanent preparations and make possible ultrastructural studies and combined applications with other procedures. In this report, we describe the production and application of a high-affinity mouse monoclonal antibody against the rate-limiting enzyme in the biosynthetic pathway of the catecholamines, tyrosine hydroxylase. This antibody, coded TOHA1.1, has been used successfully to stain tyrosine hydroxylase immunoreactive sites in the known catecholaminergic neurons and fiber systems of rat brain in both light and electron microscopy. It has also been demonstrated that TOH A1.1 will immunoprecipitate phosphorylated tyrosine hydroxylase.
利用儿茶酚胺的荧光衍生物,通过组织化学方法对神经系统中的儿茶酚胺能神经元进行了研究,并使用针对其生物合成酶的抗体进行了免疫细胞化学研究。免疫细胞化学技术可产生永久性标本,使得超微结构研究以及与其他方法的联合应用成为可能。在本报告中,我们描述了一种针对儿茶酚胺生物合成途径中的限速酶——酪氨酸羟化酶的高亲和力小鼠单克隆抗体的制备及其应用。这种编码为TOHA1.1的抗体已成功用于在光学显微镜和电子显微镜下对大鼠脑中已知的儿茶酚胺能神经元和纤维系统中的酪氨酸羟化酶免疫反应位点进行染色。还证实TOH A1.1可免疫沉淀磷酸化的酪氨酸羟化酶。