STUDIES OF HUMAN ANTI-γ-GLOBULIN FACTORS REACTING WITH PEPSIN-DIGESTED γ-GLOBULINS

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 a...

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Main Authors: Lawrence, Thomas G., Williams, Ralph C.
Format: Online
Language:English
Published: The Rockefeller University Press 1967
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138353/
id pubmed-2138353
recordtype oai_dc
spelling pubmed-21383532008-04-17 STUDIES OF HUMAN ANTI-γ-GLOBULIN FACTORS REACTING WITH PEPSIN-DIGESTED γ-GLOBULINS Lawrence, Thomas G. Williams, Ralph C. Article 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. The Rockefeller University Press 1967-01-31 /pmc/articles/PMC2138353/ /pubmed/4163708 Text en Copyright © 1967 by The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Lawrence, Thomas G.
Williams, Ralph C.
spellingShingle Lawrence, Thomas G.
Williams, Ralph C.
STUDIES OF HUMAN ANTI-γ-GLOBULIN FACTORS REACTING WITH PEPSIN-DIGESTED γ-GLOBULINS
author_facet Lawrence, Thomas G.
Williams, Ralph C.
author_sort Lawrence, Thomas G.
title STUDIES OF HUMAN ANTI-γ-GLOBULIN FACTORS REACTING WITH PEPSIN-DIGESTED γ-GLOBULINS
title_short STUDIES OF HUMAN ANTI-γ-GLOBULIN FACTORS REACTING WITH PEPSIN-DIGESTED γ-GLOBULINS
title_full STUDIES OF HUMAN ANTI-γ-GLOBULIN FACTORS REACTING WITH PEPSIN-DIGESTED γ-GLOBULINS
title_fullStr STUDIES OF HUMAN ANTI-γ-GLOBULIN FACTORS REACTING WITH PEPSIN-DIGESTED γ-GLOBULINS
title_full_unstemmed STUDIES OF HUMAN ANTI-γ-GLOBULIN FACTORS REACTING WITH PEPSIN-DIGESTED γ-GLOBULINS
title_sort studies of human anti-γ-globulin factors reacting with pepsin-digested γ-globulins
description 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.
publisher The Rockefeller University Press
publishDate 1967
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138353/
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