Wymann, Sandra; Ghielmetti, Marco; Schaub, Alexander; Baumann, Michael J; Stadler, Beda M; Bolli, Reinhard; Miescher, Sylvia M (2008). Monomerization of dimeric IgG of intravenous immunoglobulin (IVIg) increases the antibody reactivity against intracellular antigens. Molecular immunology, 45(9), pp. 2621-8. Amsterdam: Elsevier 10.1016/j.molimm.2007.12.020
Full text not available from this repository.Intravenous immunoglobulin (IVIg) preparations are derived from pooled plasma from up to 60,000 healthy human donors and reflect the immunologic experience of the donor population. IVIg contains monomeric and dimeric IgG populations which are in a dynamic equilibrium depending on concentration, pH, temperature, donor pool size, time and stabilizers added in order to keep the portion of dimeric IgG below a certain level. In the present study, monomeric and dimeric fractions were isolated by size exclusion chromatography. The dimeric fractions, however, showed a dynamic instability and tended to dissociate. Both dimeric and monomeric IgG fractions were acid treated (pH 4) in order to dissociate the dimeric IgG. Western-blot analysis identified a sub-population of SDS resistant IgG dimers. Furthermore, the reactivities of the fractions were tested against a panel of self- and exo-antigens. There was a marked increase in activity of the dimeric compared to the monomeric IgG fraction against various intracellular self-antigens. Our data indicates that the increased reactivities of pH 4-treated fractions can mainly be attributed to dimer dissociation, as pH 4-treated monomers do not show significantly increased activities against a range of antigens.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
04 Faculty of Medicine > Department of Haematology, Oncology, Infectious Diseases, Laboratory Medicine and Hospital Pharmacy (DOLS) > Institute for Immunology [discontinued] |
UniBE Contributor: |
Stadler, Beda Martin |
ISSN: |
0161-5890 |
ISBN: |
18280568 |
Publisher: |
Elsevier |
Language: |
English |
Submitter: |
Factscience Import |
Date Deposited: |
04 Oct 2013 15:04 |
Last Modified: |
05 Dec 2022 14:19 |
Publisher DOI: |
10.1016/j.molimm.2007.12.020 |
PubMed ID: |
18280568 |
Web of Science ID: |
000255528400019 |
URI: |
https://boris.unibe.ch/id/eprint/27951 (FactScience: 114405) |
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