针对牛血清白蛋白的单克隆抗体：亲和力和特异性测定

Monoclonal antibodies to bovine serum albumin: affinity and specificity determinations.

作者信息

Morel G A, Yarmush D M, Colton C K, Benjamin D C, Yarmush M L

机构信息

Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge 02139.

出版信息

Mol Immunol. 1988 Jan;25(1):7-15. doi: 10.1016/0161-5890(88)90085-5.

DOI:10.1016/0161-5890(88)90085-5

PMID:3343974

Abstract

A panel of 12 monoclonal antibodies (MAb) to bovine serum albumin (BSA) was developed and characterized as to their physiochemical and immunological properties. Affinity constants of the MAb varied over a wide range from 10(5) to 10(8) M-1. MAb were assembled into several groups of non- or minimally interacting antibodies by analysis of competitive binding experiments, and BSA domain and subdomain specificities of the MAb were assigned by analysis of results of MAb binding to purified BSA fragments. Further fine specificity delineation was accomplished by examination of cross-reactivity patterns to several mammalian albumins. The data suggest that some of the low affinity MAb recognize sites on different portions of the BSA molecule, indicating that similar epitopes exist on different domains of the BSA molecule.

摘要

开发了一组针对牛血清白蛋白（BSA）的12种单克隆抗体（MAb），并对其理化和免疫学特性进行了表征。MAb的亲和常数在10⁵至10⁸ M⁻¹的广泛范围内变化。通过竞争性结合实验分析，将MAb分为几组非相互作用或最小相互作用的抗体，并通过分析MAb与纯化的BSA片段的结合结果来确定MAb对BSA结构域和亚结构域的特异性。通过检测与几种哺乳动物白蛋白的交叉反应模式，进一步完成了精细特异性的描绘。数据表明，一些低亲和力的MAb识别BSA分子不同部分的位点，这表明BSA分子的不同结构域上存在相似的表位。