Ontology highlight
ABSTRACT:
SUBMITTER: Yang H
PROVIDER: S-EPMC3906645 | biostudies-literature | 2010 May-Jun
REPOSITORIES: biostudies-literature
Yang Haiou H Gurgel Patrick V PV Williams D Keith DK Bobay Benjamin G BG Cavanagh John J Muddiman David C DC Carbonell Ruben G RG
Journal of molecular recognition : JMR 20100501 3
Affinity ligand HWRGWV has demonstrated the ability to isolate human immunoglobulin G (hIgG) from mammalian cell culture media. The ligand specifically binds hIgG through its Fc portion. This work shows that deglycosylation of hIgG has no influence on its binding to the HWRGWV ligand and the ligand does not compete with Protein A or Protein G in binding hIgG. It is suggested by the mass spectrometry (MS) data and docking simulation that HWRGWV binds to the pFc portion of hIgG and interacts with ...[more]