Heterogeneity of human polyclonal IgE reacting with staphylococcal protein A
Language English Country United States Media print
Document type Journal Article
PubMed
6430762
DOI
10.1007/bf02877318
Knihovny.cz E-resources
- MeSH
- Chromatography, Affinity MeSH
- Immunodiffusion MeSH
- Immunoglobulin E metabolism MeSH
- Hydrogen-Ion Concentration MeSH
- Humans MeSH
- Staphylococcal Protein A metabolism MeSH
- Binding Sites, Antibody MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Immunoglobulin E MeSH
- Staphylococcal Protein A MeSH
A small part of polyclonal IgE (6%) was bound to protein A-Sepharose from the serum of M.P., containing a high concentration of IgE. No monoclonal IgE isolated from the serum of V.L. was bound to this sorbent. This binding of polyclonal IgE appears to be heterogeneous since a multiphasic pattern was observed with discontinuous pH gradient elution from protein A-Sepharose. Also, like IgE from the whole serum, monomeric IgE isolated from the serum of M.P. on Sepharose 6B showed this binding heterogeneity. It is suggested that IgE molecules with different affinities for protein A could belong to different isotypic or allotypic variants.
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