首页 | 本学科首页   官方微博 | 高级检索  
     


Mass spectrometry analysis of in vitro nitration of a recombinant human IgG1 monoclonal antibody
Authors:Liu Hongcheng  Gaza-Bulseco Georgeen  Chumsae Chris  Radziejewski Czeslaw H
Affiliation:Process Sciences Department, Abbott Bioresearch Center, 100 Research Drive, Worcester, MA 01605, USA. hongcheng.liu@abbott.com
Abstract:Nitration of a recombinant human monoclonal antibody was carried out in vitro by incubating the antibody with the nitrating reagent tetranitromethane (TNM). The susceptible sites of nitration were identified using high-performance liquid chromatography/mass spectrometry (HPLC/MS). In general, tyrosine residues in the variable domains of the antibody are more susceptible to nitration, while tyrosine residues in the constant domains are relatively resistant to nitration. However, one tyrosine residue in the CH1 domain and one tyrosine residue in the CH2 domain are highly susceptible to nitration. Interestingly, the susceptible tyrosine residue in the CH2 domain is followed by the conserved asparagine residue that is glycosylated.
Keywords:
本文献已被 PubMed 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号