Abstract
Immunoglobulin M (IgM) antibodies hold promise as anticancer drugs and as agents for promoting immune homeostasis. This promise has not been realized due to low expression levels in mammalian cells producing IgM class antibodies, and the failure of protein A chromatography for IgM purification. Here, we describe a nonchromatographic platform for quantitatively capturing IgMs at neutral pH, which is then recovered with 86%–94% yield and >95% purity at pH 3. The platform contains micelles conjugated with the [(bathophenanthroline)3:Fe2+] amphiphilic complex. Inclusion of amino acid monomers, for example, phenylalanine or tyrosine, during conjugation of detergent micelles, allows subsequent extraction of IgMs at close to neutral pH. With the successful implementation of this purification platform for both polyclonal humans and bovine IgMs, we anticipate similar results for monoclonal IgMs, most relevant for the pharmaceutical industry.
| Original language | English |
|---|---|
| Pages (from-to) | 1997-2003 |
| Number of pages | 7 |
| Journal | Biotechnology and Bioengineering |
| Volume | 119 |
| Issue number | 7 |
| Early online date | 24 Mar 2022 |
| DOIs | |
| Publication status | Published - Jul 2022 |
Funding
G.P. thanks the research authority of Ariel University for their generous support. M.S. thanks the Kimmelman Center for Biomolecular Structure and Assembly for their generous support of M.S. M.S. holds the Katzir Makineni Chair in Chemistry.