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Some properties of antisera to serum amyloid A protein (SAA): inhibition of precipitation by complexing of SAA to albumin
Three potent rabbit antisera to human serum amyloid A protein (SAA) appear to be directed exclusibely to the carboxy terminal region not shared with the tissue amyloid A protein. Since binding to albumin completely blocks the reaction of these antisera with the antigen, and since SAA exists in serum...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1976
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2190493/ https://www.ncbi.nlm.nih.gov/pubmed/63532 |
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collection | PubMed |
description | Three potent rabbit antisera to human serum amyloid A protein (SAA) appear to be directed exclusibely to the carboxy terminal region not shared with the tissue amyloid A protein. Since binding to albumin completely blocks the reaction of these antisera with the antigen, and since SAA exists in serum complexed to albumin, the anti-SAA cannot be used to detect or quantitate this serum component. The possibility that similar problems will be encountered with immunoassays for molecules that exist complexed to other proteins is discussed. |
format | Text |
id | pubmed-2190493 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1976 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21904932008-04-17 Some properties of antisera to serum amyloid A protein (SAA): inhibition of precipitation by complexing of SAA to albumin J Exp Med Articles Three potent rabbit antisera to human serum amyloid A protein (SAA) appear to be directed exclusibely to the carboxy terminal region not shared with the tissue amyloid A protein. Since binding to albumin completely blocks the reaction of these antisera with the antigen, and since SAA exists in serum complexed to albumin, the anti-SAA cannot be used to detect or quantitate this serum component. The possibility that similar problems will be encountered with immunoassays for molecules that exist complexed to other proteins is discussed. The Rockefeller University Press 1976-12-01 /pmc/articles/PMC2190493/ /pubmed/63532 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 Some properties of antisera to serum amyloid A protein (SAA): inhibition of precipitation by complexing of SAA to albumin |
title | Some properties of antisera to serum amyloid A protein (SAA): inhibition of precipitation by complexing of SAA to albumin |
title_full | Some properties of antisera to serum amyloid A protein (SAA): inhibition of precipitation by complexing of SAA to albumin |
title_fullStr | Some properties of antisera to serum amyloid A protein (SAA): inhibition of precipitation by complexing of SAA to albumin |
title_full_unstemmed | Some properties of antisera to serum amyloid A protein (SAA): inhibition of precipitation by complexing of SAA to albumin |
title_short | Some properties of antisera to serum amyloid A protein (SAA): inhibition of precipitation by complexing of SAA to albumin |
title_sort | some properties of antisera to serum amyloid a protein (saa): inhibition of precipitation by complexing of saa to albumin |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2190493/ https://www.ncbi.nlm.nih.gov/pubmed/63532 |