Many sera from normal individuals as well as patients with various disease states contain agglutinating antibodies which show specificity for antigenic determinants of γ-globulin revealed by pepsin digestion at pH 4.1. Sera containing such agglutinating activity as well as sera negative for these agglutinators contain low molecular weight (3S–5S) components of slow γ-mobility which inhibit these agglutination reactions. Low molecular weight inhibitors show both auto- and isospecificity, and are antigenically related to the 5S pepsin fragment of γ-globulin. A common situation is thereby revealed in which human anti-γ-globulin antibodies showing specificity for pepsin-digested γ-globulins are present in serum along with low molecular weight γ-globulin components capable of inhibition. Autoreactivity or autospecificity of such anti-γ-globulin factors is a phenomenon shared by both normal human sera and sera from patients with various disease states.
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1 February 1967
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February 01 1967
STUDIES OF HUMAN ANTI-γ-GLOBULIN FACTORS REACTING WITH PEPSIN-DIGESTED γ-GLOBULINS
Thomas G. Lawrence, Jr.,
Thomas G. Lawrence, Jr.
From the Arthritis Unit, the Department of Medicine, University Hospitals, Minneapolis, Minnesota
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Ralph C. Williams, Jr.
Ralph C. Williams, Jr.
From the Arthritis Unit, the Department of Medicine, University Hospitals, Minneapolis, Minnesota
Search for other works by this author on:
Thomas G. Lawrence, Jr.
From the Arthritis Unit, the Department of Medicine, University Hospitals, Minneapolis, Minnesota
Ralph C. Williams, Jr.
From the Arthritis Unit, the Department of Medicine, University Hospitals, Minneapolis, Minnesota
Received:
September 23 1966
Online ISSN: 1540-9538
Print ISSN: 0022-1007
Copyright © 1967 by The Rockefeller University Press
1967
J Exp Med (1967) 125 (2): 233–248.
Article history
Received:
September 23 1966
Citation
Thomas G. Lawrence, Ralph C. Williams; STUDIES OF HUMAN ANTI-γ-GLOBULIN FACTORS REACTING WITH PEPSIN-DIGESTED γ-GLOBULINS . J Exp Med 1 February 1967; 125 (2): 233–248. doi: https://doi.org/10.1084/jem.125.2.233
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