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The Journal of Immunology, 1976, 117: 587-593.
Copyright © 1976 by The American Association of Immunologists, Inc.

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Immunoglobulin Binding by Mouse Intestinal Epithelial Cell Receptors1

Ruth L. Guyer, Marian E. Koshland2 and Paul M. Knopf

Department of Bacteriology and Immunology, University of California, Berkeley, California 94720 and the Division of Biological and Medical Sciences, Brown University, Providence, Rhode Island 02912

Abstract

The IgG receptors involved in transporting maternal antibodies to the blood stream of the young mouse were studied by feeding internally labeled mouse myeloma proteins and enzymatically generated specific fragments of these proteins. The data obtained from competition experiments showed the following: 1) intestinal receptors have a single specificity which is directed against IgG Fc determinants; 2) IgG subclass proteins differ in their affinities for the receptors and thus have similar but not identical Fc recognition sites; 3) the order of affinities of the IgG subclass proteins for the receptors correlates with the relative concentrations of the four subclass proteins in mouse milk; and 4) several subfractions of the Fc fragment were inactive in binding to the receptors. In many of their properties the intestinal receptors resemble the Fc receptors on other cell types, but they are apparently unique in their ability to bind tightly non-aggregated IgG molecules.

Footnotes

1 This work was funded by Research Grant AI 07079 from the National Institute of Allergy and Infectious Diseases, United States Public Health Service. R. L. G. was supported by Trainee Grant AI 120 from the National Institutes of Health, U.S. Public Health Service. P. M. K. was supported by Research Grant AI 11169.

2 Please address reprint requests to Dr. Marian Koshland, Department of Bacteriology and Immunology, University of California, Berkeley, California 94720.




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