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A branched, synthetic octapeptide of ubiquitinated histone H2A as target of autoantibodies

Two peptides of eight (T2) and 10 (T1) residues corresponding to the branched moiety of ubiquitinated histone H2A have been synthesized and used for raising specific antibodies in rabbits. Antisera to peptide T1 reacted in ELISA with T1 and with H2A but not with ubiquitin; antisera to peptide T2 rea...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1989
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189308/
https://www.ncbi.nlm.nih.gov/pubmed/2541220
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description Two peptides of eight (T2) and 10 (T1) residues corresponding to the branched moiety of ubiquitinated histone H2A have been synthesized and used for raising specific antibodies in rabbits. Antisera to peptide T1 reacted in ELISA with T1 and with H2A but not with ubiquitin; antisera to peptide T2 reacted with T2 but not with H2A or ubiquitin. When tested in immunoblotting, both peptide antisera reacted with ubiquitinated H2A but not with unconjugated H2A or with ubiquitin. Sera from patients with systemic lupus erythematosus (SLE) were shown previously to react with ubiquitin in ELISA and immunoblotting. When tested for their ability to react in ELISA with synthetic peptides T1 and T2, 96% of the SLE sera (diluted 1:500) that recognized ubiquitin also reacted with peptide T2. Of the SLE sera that did not react with ubiquitin, only 13% possessed antibodies able to bind peptide T2. Antibodies from seven SLE sera, purified on a T2-immunoadsorbent column, were also able to react either with H2A, and in three cases also with ubiquitin.
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spelling pubmed-21893082008-04-17 A branched, synthetic octapeptide of ubiquitinated histone H2A as target of autoantibodies J Exp Med Articles Two peptides of eight (T2) and 10 (T1) residues corresponding to the branched moiety of ubiquitinated histone H2A have been synthesized and used for raising specific antibodies in rabbits. Antisera to peptide T1 reacted in ELISA with T1 and with H2A but not with ubiquitin; antisera to peptide T2 reacted with T2 but not with H2A or ubiquitin. When tested in immunoblotting, both peptide antisera reacted with ubiquitinated H2A but not with unconjugated H2A or with ubiquitin. Sera from patients with systemic lupus erythematosus (SLE) were shown previously to react with ubiquitin in ELISA and immunoblotting. When tested for their ability to react in ELISA with synthetic peptides T1 and T2, 96% of the SLE sera (diluted 1:500) that recognized ubiquitin also reacted with peptide T2. Of the SLE sera that did not react with ubiquitin, only 13% possessed antibodies able to bind peptide T2. Antibodies from seven SLE sera, purified on a T2-immunoadsorbent column, were also able to react either with H2A, and in three cases also with ubiquitin. The Rockefeller University Press 1989-05-01 /pmc/articles/PMC2189308/ /pubmed/2541220 Text en 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/).
spellingShingle Articles
A branched, synthetic octapeptide of ubiquitinated histone H2A as target of autoantibodies
title A branched, synthetic octapeptide of ubiquitinated histone H2A as target of autoantibodies
title_full A branched, synthetic octapeptide of ubiquitinated histone H2A as target of autoantibodies
title_fullStr A branched, synthetic octapeptide of ubiquitinated histone H2A as target of autoantibodies
title_full_unstemmed A branched, synthetic octapeptide of ubiquitinated histone H2A as target of autoantibodies
title_short A branched, synthetic octapeptide of ubiquitinated histone H2A as target of autoantibodies
title_sort branched, synthetic octapeptide of ubiquitinated histone h2a as target of autoantibodies
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189308/
https://www.ncbi.nlm.nih.gov/pubmed/2541220