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The Journal of Immunology, 1962, 88: 229-239.
Copyright © 1962 by The American Association of Immunologists, Inc.

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Studies on Organ Specificity

XIII. Immunological Analysis of Thyroglobulin and Thyralbumin1

Noel R. Rose, Sidney Shulman2 and Ernest Witebsky

Department of Bacteriology and Immunology, University of Buffalo School of Medicine, Buffalo, New York

Abstract

1. Hog thyroid crude extract and two fractions derived from it by ammonium sulfate precipitation—thyroglobulin and thyralbumin—were evaluated serologically, using rabbit antisera with various combinations of thyroid-specific and species-specific antibodies. Most of the organ specific thyroid antigen is precipitated as thyroglobulin between 1.60 and 1.70 M ammonium sulfate. Very little species-specific antigen precipitates in this fraction. Additional thyroid-specific antigens that do not cross-react with antiserum to heterologous beef thyroid extract are brought down by higher levels of ammonium sulfate.
2. The thyralbumin fraction, precipitated between 2.50 and 3.00 M ammonium sulfate, contains little or no detectable thyroglobulin but reacts strongly with hog serum antiserum. Absorption of antithyralbumin rabbit serum with hog serum removes all of its demonstrable antibody content.
3. In double diffusion gel precipitation tests, with thyralbumin antiserum, thyralbumin produces up to four lines, all identical with antigens of hog serum or hog kidney. By means of immunoelectrophoresis, thyralbumin can be seen to contain at least two components, migrating with mobilities of serum albumin and serum {gamma}-globulin respectively. In the same experiment, thyroglobulin appears as a single or doubled are in the {alpha}-globulin region.

Footnotes

Supported in part by Research Grants C-2357 and C-3737 from the National Cancer Institute of the National Institutes of Health, Public Health Service.

2 Supported by a Senior Research Fellowship (SF-118) from the Public Health Service.







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