去酰胺
天冬酰胺
化学
单克隆抗体
重组DNA
抗原
抗体
生物化学
分子生物学
残留物(化学)
酶
免疫学
生物
基因
作者
Christian Nowak,Akash Tiwari,Hongcheng Liu
标识
DOI:10.1021/acs.analchem.8b01322
摘要
Asparagine deamidation in the complementarity determining regions of recombinant monoclonal antibodies has been extensively studied and shown to have a negative impact on antigen binding. Those asparagine residues are typically exposed and thus have a higher tendency toward deamidation, depending also on local structure and environmental factors such as temperature and pH. Deamidation rates and products of a susceptible asparagine residue in the complementarity determining regions of a recombinant monoclonal antibody free in solution or in the antibody–antigen complex were studied. The results demonstrated that incubation of the antibody or its antigen complex generated a similar amount of aspartate. The expected amount of isoaspartate product was detected in free antibody, but it was completely lacking in the antibody–antigen complex.
科研通智能强力驱动
Strongly Powered by AbleSci AI