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Folia Microbiologica

, Volume 29, Issue 3, pp 264–268 | Cite as

Heterogencity of human polyclonal IgE reacting with staphylococcal protein A

  • J. Zikán
  • V. Zavázal
  • V. Krauz
Article

Abstract

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.

Keywords

Staphylococcal Protein Allotypic Marker Allotypic Variant Multiphasic Pattern Single Radial Diffusion 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Institute of Microbiology, Academy of Sciences of the Czech Republic 1984

Authors and Affiliations

  • J. Zikán
    • 1
  • V. Zavázal
    • 2
  • V. Krauz
    • 2
  1. 1.Institute of MicrobiologyCzechoslovak Academy of SciencesPrague 4
  2. 2.Faculty of MedicineCharles UniversityPilsenCzechoslovakia

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