Identification of IgE Journal of Allergy and Clinical Immunology

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Presentation transcript:

Identification of IgE Journal of Allergy and Clinical Immunology Kimishige Ishizaka, MD, PhD, Teruko Ishizaka, MD, PhD Journal of Allergy and Clinical Immunology Volume 137, Issue 6, Pages 1646-1650 (June 2016) DOI: 10.1016/j.jaci.2015.12.1343 Copyright © 2016 The Authors Terms and Conditions

Fig 1 Detection of anti-reagin antibodies by PK reactions. For passive sensitization, 0.05 mL of 1:100 (bottom) to 1:800 (top) dilutions of a mixture of the patient's serum with either antiserum (Abs) or normal rabbit serum (Cont) were injected (see text). Journal of Allergy and Clinical Immunology 2016 137, 1646-1650DOI: (10.1016/j.jaci.2015.12.1343) Copyright © 2016 The Authors Terms and Conditions

Fig 2 Distribution of γE antibodies against ragweed antigen in chromatographic fractions of the sera of ragweed-sensitive patients from the DEAE cellulose column. Stepwise elution was made with 0.005 mol/L (I), 0.025 mol/L (II), 0.035 mol/L (III), 0.05 mol/L (IV), and 0.08 mol/L (V) phosphate buffers, pH 8.0. S, Original serum. The center well of the agarose plate was filled with anti-reagin (γE) antiserum, followed by 131I-labeled ragweed antigen E. Journal of Allergy and Clinical Immunology 2016 137, 1646-1650DOI: (10.1016/j.jaci.2015.12.1343) Copyright © 2016 The Authors Terms and Conditions

Fig 3 Radioimmunoelectrophoresis of the reagin-rich fraction of the serum of a ragweed-sensitive patient with hay fever. After electrophoresis, the trough was filled with anti-γE, followed by 131I-labeled ragweed antigen E. Both the stained slide (top) and autoradiograph (bottom) are shown. Journal of Allergy and Clinical Immunology 2016 137, 1646-1650DOI: (10.1016/j.jaci.2015.12.1343) Copyright © 2016 The Authors Terms and Conditions

Fig 4 Radioimmunodiffusion analysis of γE isolated from the serum of a ragweed-sensitive patient. The center well was filled with purified γE. Peripheral wells were filled with the antiserum specific for each immunoglobulin isotype, followed by 131I-labeled ragweed antigen E. Both the stained slide (left) and autoradiograph (right) are shown. Journal of Allergy and Clinical Immunology 2016 137, 1646-1650DOI: (10.1016/j.jaci.2015.12.1343) Copyright © 2016 The Authors Terms and Conditions

Fig 5 Antigenic identity of γE and myeloma protein ND. Purified γE from the sera of ragweed-sensitive patients was placed in the center well. Peripheral wells were filled with the antiserum specific for ND protein and the antibodies specific for each human immunoglobulin isotype, followed by 131I-labeled ragweed antigen E. Journal of Allergy and Clinical Immunology 2016 137, 1646-1650DOI: (10.1016/j.jaci.2015.12.1343) Copyright © 2016 The Authors Terms and Conditions

Fig 6 Identification of IgE on human basophilic granulocytes: autoradiograph of normal human leukocytes treated with 125I-labeled anti-IgE. Journal of Allergy and Clinical Immunology 2016 137, 1646-1650DOI: (10.1016/j.jaci.2015.12.1343) Copyright © 2016 The Authors Terms and Conditions

Fig 7 Selective binding of IgE on monkey mast cells. E myeloma protein PS was injected intracutaneously into a monkey. Twenty-four hours later, the skin tissues were treated with 125I-labeled anti-IgE, and frozen sections of the tissues were examined. Both the stained slide (bottom) and autoradiograph (top) are shown. Journal of Allergy and Clinical Immunology 2016 137, 1646-1650DOI: (10.1016/j.jaci.2015.12.1343) Copyright © 2016 The Authors Terms and Conditions