Al-Bassam M N, O'Sullivan M J, Gnemmi E, Bridges J W, Marks V
Clin Chem. 1978 Sep;24(9):1590-4.
beta-D-Galactosidase (EC 3.2.1.23) from Escherichia coli was conjugated to desmethylnortriptyline by means of a bifunctional cross-linking reagent, dimethyl adipimidate, and used in a double-antibody immunoassay for nortriptyline. Eighty percent of the enzyme activity was retained after conjugation; 75% of the enzyme was conjugated to desmethylnortriptyline. In the final immunoassay the enzyme activity of the bound fraction was determined with o-nitrophenyl-beta-D-galactopyranoside as substrate. The sensitivity, precision, and simplicity of the enzyme immunoassay compared favorable with that of a published radioimmunoassay method. Results for nortriptyline in plasma samples correlated well with those determined by either radioimmunoassay or gas-chromatography.
利用双功能交联剂己二酸二甲酯将来自大肠杆菌的β-D-半乳糖苷酶(EC 3.2.1.23)与去甲替林进行偶联,并将其用于去甲替林的双抗体免疫测定。偶联后保留了80%的酶活性;75%的酶与去甲替林偶联。在最终的免疫测定中,以邻硝基苯基-β-D-吡喃半乳糖苷为底物测定结合部分的酶活性。与已发表的放射免疫测定方法相比,酶免疫测定的灵敏度、精密度和简便性具有优势。血浆样本中去甲替林的检测结果与放射免疫测定法或气相色谱法测定的结果相关性良好。