文献类型：期刊文献

中文题名：免疫球蛋白G-葡萄糖脱氢酶结合物的研究

英文题名：Study on IgG-Glucosedehydrogenase Conjugates

作者：杨曜中[1];金新根[1]

机构：[1]华东化工学院生化工程系

年份：1992

卷号：18

期号：3

起止页码：296

中文期刊名：华东化工学院学报

收录：国家哲学社会科学学术期刊数据库;Scopus;CSCD:【CSCD2011_2012】；

语种：中文

中文关键词：脱氢酶;巯基;葡萄糖;免疫球蛋白G

外文关键词：immunoglobulin G; dehydrogenase; sulfhydryl group; conjugates; IgG-glucosedehydrogenase

摘要：介绍一种新的酶结合物的制备方法,研究了该结合物在酶联免疫吸附测定中的初步应用。通过2-亚氨硫杂戊烷的修饰反应,在葡萄糖脱氢酶、抗体(IgG)分子上分别引入新的游离巯基。巯基化的葡萄糖脱氢酶和免疫球蛋白G之间,通过双功能试剂二马来酰亚胺甲醚(进行)偶联,偶联产物由Sephacryl S-300柱层析纯化。按非竞争性固相双抗体夹心法,将精制的IgG-葡萄糖脱氢酶(A)结合物用于人白蛋白(Ⅰ),人甲胎蛋白(Ⅱ)和牛胰岛素(Ⅲ)的定量检测。在0～10 ng/mL范围内,Ⅰ和Ⅱ与A活性均呈良好的线性相关;但Ⅲ与A活性之间没有任何相应关系。
The preparation of new enzyme conjugates and its initial application in ELISA were discussed. New free sulfhydryl were separately introduced into the antibody (IgG) and glucosedehydrogenase by the modification of 2-iminothiolane. The thiolated amino group of IgG and glucosedehydrogenase conjugates, by using a bifunctional BMME. The conjugates were purified through Sephacryl S-300 column chromotography. The purified IgG-glucosedehydrogenase were used for the quantitative analysis with non-competitive solid phase doubleantibody sandwish method. There are good linear relations between the amount of human albumin or human AFP and the enzyme activity of conjugates within the range of 0～10 ng/ml, but not any relations between bovine insulin and conjugates.