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The Journal of Immunology, 1968, 100: 612-621.
Copyright © 1968 by The American Association of Immunologists, Inc.

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Specificity of Antiglobulin Factors in Normal Human Serum Reacting with Enzyme Digested {gamma}G-Globulin1

Lucy C. Kormeier2, Judy T. Ing and William J. Mandy3

From the Department of Microbiology, The University of Texas, Austin, Texas

Abstract

Papain agglutinator in normal human serum was found to react with erythrocytes sensitized with autologous and homologous Fab fragments of anti-Rh antibody. The incidence of agglutinator activity ranged from 24 to 93%. This broad range was attributed to the sensitivity of the hemagglutination assay, specificity of Fab sensitizor, age of the individuals and parental background.

Papain agglutinator is similar to the previously described pepsin agglutinator in many respects, but differences in specificity were established by reciprocal absorption and inhibition experiments. Therefore a new buried antigenic determinant is exposed by digesting human {gamma}G-globulin with papain. This antigenic difference between the Fab and (Fab')2 fragments supports the concept that papain and pepsin cleaves the {gamma}G-globulin molecules at different sites.

Footnotes

This investigation was supported by a United States Public Health Service Grant, AI-07184-03.

2 Recipient of a United States Public Health Service Predoctoral Training Grant Fellowship.

3 Recipient of a United States Public Health Service Career Development Award, 1-K3-GM-21, 252-01.




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