一种用于亲和纯化放射性标记单克隆抗体的简单方法。

A simple method for affinity purification of radiolabeled monoclonal antibodies.

作者信息

Juweid M, Sato J, Paik C, Onay-Basaran S, Weinstein J N, Neumann R D

机构信息

Department of Nuclear Medicine, National Cancer Institute, NIH, Bethesda, MD 20892.

出版信息

Nucl Med Biol. 1993 Apr;20(3):311-5. doi: 10.1016/0969-8051(93)90053-w.

DOI:10.1016/0969-8051(93)90053-w

PMID:8485490

Abstract

A simple method is described for affinity purification of radiolabeled antibodies using glutaraldehyde-fixed tumor target cells. The cell-bound antibody fraction is removed from the cells by an acid wash and then immediately subjected to buffer-exchange chromatography. The method was applied to the D3 murine monoclonal antibody which binds to a 290 kDa antigen on the surface of Line 10 guinea pig carcinoma cells. No alteration in the molecular size profile was detected after acid washing. Purification resulted in a significant increase in immunoreactivity by an average of 14 +/- 47% (SD; range 4-30%).

摘要

本文描述了一种使用戊二醛固定的肿瘤靶细胞亲和纯化放射性标记抗体的简单方法。通过酸洗从细胞中去除细胞结合的抗体部分，然后立即进行缓冲液交换色谱。该方法应用于D3鼠单克隆抗体，其与10号线豚鼠癌细胞表面的290 kDa抗原结合。酸洗后未检测到分子大小分布的改变。纯化后免疫反应性显著增加，平均增加14±47%（标准差；范围4-30%）。