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THE CONVERSION OF C'1S TO C'1 ESTERASE BY PLASMIN AND TRYPSIN
The formation of C'1 esterase from C'1, the first component of complement, may be brought about by the action of plasmin or trypsin upon C'1s, a subcomponent of C'1. These enzymes also decrease the esterolytic activity of C'1 esterase. The formation of C'1 esterase was...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1967
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138350/ https://www.ncbi.nlm.nih.gov/pubmed/4225264 |
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author | Ratnoff, Oscar D. Naff, George B. |
author_facet | Ratnoff, Oscar D. Naff, George B. |
author_sort | Ratnoff, Oscar D. |
collection | PubMed |
description | The formation of C'1 esterase from C'1, the first component of complement, may be brought about by the action of plasmin or trypsin upon C'1s, a subcomponent of C'1. These enzymes also decrease the esterolytic activity of C'1 esterase. The formation of C'1 esterase was demonstrated by measuring the appearance of an agent or agents with esterolytic properties and the capacity to inactivate C'2 and C'4, attributes of C'1 esterase. The activity of the agent which evolved was blocked by serum inhibitor of C'1 esterase. The implications of these observations, that the formation of C'1 esterase during complement fixation is mediated by proteolytic processes, are under study. The possible inhibition of C'1q by soybean trypsin inhibitor is in agreement with this hypothesis. |
format | Text |
id | pubmed-2138350 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1967 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21383502008-04-17 THE CONVERSION OF C'1S TO C'1 ESTERASE BY PLASMIN AND TRYPSIN Ratnoff, Oscar D. Naff, George B. J Exp Med Article The formation of C'1 esterase from C'1, the first component of complement, may be brought about by the action of plasmin or trypsin upon C'1s, a subcomponent of C'1. These enzymes also decrease the esterolytic activity of C'1 esterase. The formation of C'1 esterase was demonstrated by measuring the appearance of an agent or agents with esterolytic properties and the capacity to inactivate C'2 and C'4, attributes of C'1 esterase. The activity of the agent which evolved was blocked by serum inhibitor of C'1 esterase. The implications of these observations, that the formation of C'1 esterase during complement fixation is mediated by proteolytic processes, are under study. The possible inhibition of C'1q by soybean trypsin inhibitor is in agreement with this hypothesis. The Rockefeller University Press 1967-01-31 /pmc/articles/PMC2138350/ /pubmed/4225264 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/). |
spellingShingle | Article Ratnoff, Oscar D. Naff, George B. THE CONVERSION OF C'1S TO C'1 ESTERASE BY PLASMIN AND TRYPSIN |
title | THE CONVERSION OF C'1S TO C'1 ESTERASE BY PLASMIN AND TRYPSIN |
title_full | THE CONVERSION OF C'1S TO C'1 ESTERASE BY PLASMIN AND TRYPSIN |
title_fullStr | THE CONVERSION OF C'1S TO C'1 ESTERASE BY PLASMIN AND TRYPSIN |
title_full_unstemmed | THE CONVERSION OF C'1S TO C'1 ESTERASE BY PLASMIN AND TRYPSIN |
title_short | THE CONVERSION OF C'1S TO C'1 ESTERASE BY PLASMIN AND TRYPSIN |
title_sort | conversion of c'1s to c'1 esterase by plasmin and trypsin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138350/ https://www.ncbi.nlm.nih.gov/pubmed/4225264 |
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