Increasing immunoglobulin G adsorption in dextran-grafted protein A gels.

ABSTRACT: The formation of a stable spatial arrangement of protein A ligands is a great challenge for the development of high-capacity polymer-grafted protein A adsorbents due to the complexity in interplay between coupled ligands and polymer chain. In this work, carboxymethyl dextrans (CMDs) with different molecular weight were introduced to provide stable spatial ligand arrangement in CMD-grafted protein A gels to improve IgG adsorption. The result showed that coupling of protein A ligand in CMD-grafted layer had no marked influence on pore size and dextran layers coupled with the ligands were stable in experimental range of salt concentrations. The result of IgG adsorption revealed that carboxymethyl dextran T10, a short CMD, was more suitable as a scaffold for the synthesis of high-capacity prot

SUBMITTER: Huan L 

PROVIDER: S-EPMC8182282 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature