Heterogeneity of human polyclonal IgE reacting with staphylococcal protein A

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...

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Bibliographic Details
Published in:Folia microbiologica 1984, Vol.29 (3), p.264-268
Main Authors: ZIKAN, J, ZAVAZAL, V, KRAUZ, V
Format: Article
Language:English
Subjects:
Antibodies, immunoglobulins
Binding Sites, Antibody
Biological and medical sciences
Chromatography, Affinity
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Humans
Hydrogen-Ion Concentration
Immunodiffusion
Immunoglobulin E - metabolism
Molecular immunology
Staphylococcal Protein A - metabolism
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Summary: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.
ISSN:0015-5632
1874-9356
DOI:10.1007/BF02877318