DOI: 10.4049/jimmunol.97.1.75. Physico-Chemical Properties of Human Reaginic Antibody

Physico-Chemical Properties of Human Reaginic Antibody

10.4049/jimmunol.97.1.75

Crossref journal-article

Oxford University Press (OUP)

The Journal of Immunology (286)

Abstract

Summary The reaginic activity in sera from ragweed-sensitive patients was inactivated after the precipitation of serum proteins with the rabbit antihuman globulin serum which did not contain any of the antibodies specific for γG-, γA-, γM-globulins and for light chains of immunoglobulins. The rabbit antiserum gave a γ1-globulin precipitin band with the reagin-containing fraction which contained γA but none of the γG-, γM- or γD-globulins. The specificity of the precipitin band was different from the γA-anti-γA band. By radioimmunoelectrophoresis and by radioimmunodiffusion, the antibody against ragweed pollen-extract (antigen E) was detected in the γ1-globulin, indicating the presence of a unique γ1-immunoglobulin. The protein was tentatively designated γE-globulin. Precipitation of γE-globulin anti-ragweed antibody in the reagincontaining fraction was accompanied by the loss of reaginic activity, whereas the precipitation of the γA-globulin antibody in the fraction did not result in any decrease of reaginic activity. The results highly suggest that the reaginic activity is associated with γE-globulin.

Bibliography

Ishizaka, K., Ishizaka, T., & Hornbrook, M. M. (1966). Physico-Chemical Properties of Human Reaginic Antibody. The Journal of Immunology, 97(1), 75â85.

Authors 3

Kimishige Ishizaka (first)
Teruko Ishizaka (additional)
Margaret M Hornbrook (additional)

References 0 Referenced 356

None

Dates

Type	When
Created	2 years, 7 months ago (Jan. 1, 2023, 11:52 a.m.)
Deposited	4 months, 3 weeks ago (April 7, 2025, 2:16 a.m.)
Indexed	3 weeks ago (Aug. 7, 2025, 4:31 p.m.)
Issued	59 years, 1 month ago (July 1, 1966)
Published	59 years, 1 month ago (July 1, 1966)
Published Online	59 years, 1 month ago (July 1, 1966)
Published Print	59 years, 1 month ago (July 1, 1966)

Funders 0

None

BibTeX

@article{Ishizaka_1966, title={Physico-Chemical Properties of Human Reaginic Antibody}, volume={97}, ISSN={0022-1767}, url={http://dx.doi.org/10.4049/jimmunol.97.1.75}, DOI={10.4049/jimmunol.97.1.75}, number={1}, journal={The Journal of Immunology}, publisher={Oxford University Press (OUP)}, author={Ishizaka, Kimishige and Ishizaka, Teruko and Hornbrook, Margaret M}, year={1966}, month=jul, pages={75–85} }

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  "abstract": "<jats:title>Summary</jats:title>\n               <jats:p>The reaginic activity in sera from ragweed-sensitive patients was inactivated after the precipitation of serum proteins with the rabbit antihuman globulin serum which did not contain any of the antibodies specific for \u03b3G-, \u03b3A-, \u03b3M-globulins and for light chains of immunoglobulins. The rabbit antiserum gave a \u03b31-globulin precipitin band with the reagin-containing fraction which contained \u03b3A but none of the \u03b3G-, \u03b3M- or \u03b3D-globulins. The specificity of the precipitin band was different from the \u03b3A-anti-\u03b3A band. By radioimmunoelectrophoresis and by radioimmunodiffusion, the antibody against ragweed pollen-extract (antigen E) was detected in the \u03b31-globulin, indicating the presence of a unique \u03b31-immunoglobulin. The protein was tentatively designated \u03b3E-globulin. Precipitation of \u03b3E-globulin anti-ragweed antibody in the reagincontaining fraction was accompanied by the loss of reaginic activity, whereas the precipitation of the \u03b3A-globulin antibody in the fraction did not result in any decrease of reaginic activity. The results highly suggest that the reaginic activity is associated with \u03b3E-globulin.</jats:p>",
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