中文摘要：

采用免疫亲和分离与质谱分析相结合的方法，对β2-微球蛋白抗原表位进行了系统研究．完整的抗原分子和已固定在载体（CNBr-activated Sepharose beads）上的单克隆抗体发生免疫亲和反应后，用Endoproteinase Glu—C，Trypsin，Aminopeptidase M和carboxypeptidase Y四种不同的蛋白酶依次酶解抗原分子，并采用基质辅助激光解析电离飞行时间质谱（MALDI—TOF—MS）技术对与抗体连接受保护而未发生水解的肽段进行了研究．结果表明：β2-微球蛋白抗原表位位于整个蛋白分子氨基酸序列的61～67位，即为SFYLLYY．通过合成肽段的分析，证明了SFYLLYY即为抗原表位，与亲和质谱方法分析结果一致．

英文摘要：

The approach for epitope mapping is the application of immunoaffinity separation and matrix assisted laser desorption/ionization （MALDI） mass spectrometry （MS）. The epitope of β2-microglobulin was identified with this approach. The antigen β2-microglobulin was coupled to a monoclonal antibody, which was covalently immobilized on a cyanogen bromide （CNBr）-activated Sepharose bead. Consecutive digestion of the antigen with endoproteinase GIu-C, trypsin, aminopeptidase M and carboxypeptidase Y resulted in affinity-bound peptides containing epitope. The bound peptides were identified by MALDI-TOF MS. The epitope recognized by the monoclonal antibody was identified to be the peptide fragment 61-67 with the sequence SFYLLYY. Synthesized peptide indicated the same result.