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The Journal of Immunology, 1967, 99: 695-702.
Copyright © 1967 by The American Association of Immunologists, Inc.

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An Antigenic Determinant of Human {gamma}G-Globulin Susceptible to Papain Digestion1

Christopher S. Henney and Kimishige Ishizaka

From the Children's Asthma Research Institute and Hospital, Denver, Colorado

Abstract

An antigenic determinant in human {gamma}G-globulin (HGG) is described which is susceptible to papain digestion. Both {gamma}1- and {gamma}2-antibodies against this determinant are readily shown in guinea pigs which have been rendered tolerant to papain digested HGG and immunized with the intact HGG molecule. Normal guinea pigs immunized solely with HGG, however, also possess antibodies against this determinant, but to a less marked degree.

The determinant is specific for the {gamma}-type of heavy chain of human {gamma}G-globulin. {gamma}G-globulin preparations from a number of other species; human {gamma}A- and {gamma}M-immunoglobulins; Bence-Jones proteins types K and L and light chain preparations from normal human {gamma}G-globulin, all lack the antigenic determinant. It was present in all of the {gamma}G-myeloma proteins tested, however, including representatives of the {gamma}G1-, {gamma}G2-, {gamma}G3- and {gamma}G4-subclasses and was also found in isolated {gamma}-chain preparations from normal {gamma}G-globulin.

The determinant is destroyed by papain and pepsin digestion, and evidence is presented to indicate that the site is essentially composed of secondary and tertiary structural forces.

Footnotes

This work was supported by Research Grant AI-04985 from the United States Public Health Service. One of us (C. S. H.) wishes to acknowledge receipt of a travel grant from the Wellcome Foundation. This paper was presented in part before the American Association of Immunologists in Chicago, April 1967.







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