The membrane attack mechanism of complement: the three polypeptide chain structure of the eigth component (C8)

The purification of human C8 in milligram quantities from outdated human serum was achieved by ammonium sulfate precipitation (37.5-50% saturation) and ion exchange column chromatography employing CM-32 cellulose and QAE-Sephadex. The yield of C8 activity ranged from 2-9%, and the average purificati...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1976
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Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2190193/
https://www.ncbi.nlm.nih.gov/pubmed/1262784
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collection PubMed
description The purification of human C8 in milligram quantities from outdated human serum was achieved by ammonium sulfate precipitation (37.5-50% saturation) and ion exchange column chromatography employing CM-32 cellulose and QAE-Sephadex. The yield of C8 activity ranged from 2-9%, and the average purification was 1,700-fold. Fully reduced C8 was shown by SDS polyacrylamide gel electrophoresis to have three polypeptide chains which were present in equimolor ratios: alpha, 77,000 daltons; beta, 63,000 daltons; and gamma, 13,700 daltons. C8 denaturation by SDS and urea in the absence of reducing agents revealed two noncovalently linked subunits: alpha-gamma, 99,000 daltons, and beta, 75,000 daltons.
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spelling pubmed-21901932008-04-17 The membrane attack mechanism of complement: the three polypeptide chain structure of the eigth component (C8) J Exp Med Articles The purification of human C8 in milligram quantities from outdated human serum was achieved by ammonium sulfate precipitation (37.5-50% saturation) and ion exchange column chromatography employing CM-32 cellulose and QAE-Sephadex. The yield of C8 activity ranged from 2-9%, and the average purification was 1,700-fold. Fully reduced C8 was shown by SDS polyacrylamide gel electrophoresis to have three polypeptide chains which were present in equimolor ratios: alpha, 77,000 daltons; beta, 63,000 daltons; and gamma, 13,700 daltons. C8 denaturation by SDS and urea in the absence of reducing agents revealed two noncovalently linked subunits: alpha-gamma, 99,000 daltons, and beta, 75,000 daltons. The Rockefeller University Press 1976-05-01 /pmc/articles/PMC2190193/ /pubmed/1262784 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
The membrane attack mechanism of complement: the three polypeptide chain structure of the eigth component (C8)
title The membrane attack mechanism of complement: the three polypeptide chain structure of the eigth component (C8)
title_full The membrane attack mechanism of complement: the three polypeptide chain structure of the eigth component (C8)
title_fullStr The membrane attack mechanism of complement: the three polypeptide chain structure of the eigth component (C8)
title_full_unstemmed The membrane attack mechanism of complement: the three polypeptide chain structure of the eigth component (C8)
title_short The membrane attack mechanism of complement: the three polypeptide chain structure of the eigth component (C8)
title_sort membrane attack mechanism of complement: the three polypeptide chain structure of the eigth component (c8)
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2190193/
https://www.ncbi.nlm.nih.gov/pubmed/1262784

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