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通过“双层包裹”实现单克隆抗体的稳定化及表面修饰

Stabilization and surface modification of monoclonal antibodies by 'bi-layer encagement'.

作者信息

Ron E, Freeman A, Solomon B

机构信息

Department of Molecular Microbiology and Biotechnology, Faculty of Life Sciences, Tel-Aviv University, Israel.

出版信息

J Immunol Methods. 1995 Mar 27;180(2):237-45. doi: 10.1016/0022-1759(94)00340-3.

Abstract

A two step simple procedure for antibody stabilization in soluble form was developed. The antibody is first treated with low molecular weight polyaldehyde (polyglutaraldehyde). Following removal of non-bound polyaldehyde the antibody-polyaldehyde conjugate is crosslinked by polyamine (alkyl amine derivative of polyglutaraldehyde). Feasibility studies were successfully conducted employing monoclonal antibody raised against horseradish peroxidase as model system. The stabilized antibody preparation exhibited improved thermal stability, enhanced resistance to proteolytic digestion and higher 'specific binding activity' in ELISA test, without losing its capability to bind large antigen (enzyme) or being recognized by another antibody (goat anti-mouse IgG).

摘要

开发了一种将抗体稳定为可溶形式的两步简单程序。首先用低分子量聚醛(聚戊二醛)处理抗体。去除未结合的聚醛后,抗体 - 聚醛缀合物通过多胺(聚戊二醛的烷基胺衍生物)交联。以抗辣根过氧化物酶单克隆抗体作为模型系统成功进行了可行性研究。稳定化的抗体制剂在ELISA试验中表现出改善的热稳定性、增强的抗蛋白水解消化能力和更高的“特异性结合活性”,同时不丧失其结合大抗原(酶)的能力或不被另一种抗体(山羊抗小鼠IgG)识别。

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