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C3 PROACTIVATOR CONVERTASE AND ITS MODE OF ACTION

The activity in human serum which is responsible for conversion of C3 proactivator (C3PA) to C3 activator was shown to reside in a 3S α-globulin. The factor, called C3PA convertase (C3PAse), was obtained in partially purified form. For conversion of C3PA, C3PAse required participation of metal ions...

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Detalles Bibliográficos
Autores principales: Müller-Eberhard, Hans J., Götze, Otto
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1972
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139164/
https://www.ncbi.nlm.nih.gov/pubmed/4111773
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author Müller-Eberhard, Hans J.
Götze, Otto
author_facet Müller-Eberhard, Hans J.
Götze, Otto
author_sort Müller-Eberhard, Hans J.
collection PubMed
description The activity in human serum which is responsible for conversion of C3 proactivator (C3PA) to C3 activator was shown to reside in a 3S α-globulin. The factor, called C3PA convertase (C3PAse), was obtained in partially purified form. For conversion of C3PA, C3PAse required participation of metal ions and of a C3 fragment, which in physicochemical and antigenic properties resembled C3b. Isolated, native C3 failed to substitute for the fragment, but did restore the impaired C3 activator system in hydrazine-treated serum. Unlike native C3, the C3 fragment initiated conversion of C3PA in whole serum. A hypothetical concept which envisions the C3 fragment as effector of C3PAse has been proposed.
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spelling pubmed-21391642008-04-17 C3 PROACTIVATOR CONVERTASE AND ITS MODE OF ACTION Müller-Eberhard, Hans J. Götze, Otto J Exp Med Brief Definitive Reports The activity in human serum which is responsible for conversion of C3 proactivator (C3PA) to C3 activator was shown to reside in a 3S α-globulin. The factor, called C3PA convertase (C3PAse), was obtained in partially purified form. For conversion of C3PA, C3PAse required participation of metal ions and of a C3 fragment, which in physicochemical and antigenic properties resembled C3b. Isolated, native C3 failed to substitute for the fragment, but did restore the impaired C3 activator system in hydrazine-treated serum. Unlike native C3, the C3 fragment initiated conversion of C3PA in whole serum. A hypothetical concept which envisions the C3 fragment as effector of C3PAse has been proposed. The Rockefeller University Press 1972-03-31 /pmc/articles/PMC2139164/ /pubmed/4111773 Text en Copyright © 1972 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/).
spellingShingle Brief Definitive Reports
Müller-Eberhard, Hans J.
Götze, Otto
C3 PROACTIVATOR CONVERTASE AND ITS MODE OF ACTION
title C3 PROACTIVATOR CONVERTASE AND ITS MODE OF ACTION
title_full C3 PROACTIVATOR CONVERTASE AND ITS MODE OF ACTION
title_fullStr C3 PROACTIVATOR CONVERTASE AND ITS MODE OF ACTION
title_full_unstemmed C3 PROACTIVATOR CONVERTASE AND ITS MODE OF ACTION
title_short C3 PROACTIVATOR CONVERTASE AND ITS MODE OF ACTION
title_sort c3 proactivator convertase and its mode of action
topic Brief Definitive Reports
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139164/
https://www.ncbi.nlm.nih.gov/pubmed/4111773
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