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STUDIES ON THE ACTIVATION OF A PROESTERASE ASSOCIATED WITH PARTIALLY PURIFIED FIRST COMPONENT OF HUMAN COMPLEMENT

It has been found that under a wide range of physico-chemical conditions a positive correlation exists between the rate of disappearance of hemolytically active, partially purified first component of human complement and the rate of activation of an esterase hydrolyzing N-acetyl-L-tyrosine ethyl est...

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Detalles Bibliográficos
Autores principales: Lepow, Irwin H., Ratnoff, Oscar D., Levy, Lawrence R.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1958
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2136687/
https://www.ncbi.nlm.nih.gov/pubmed/13513912
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author Lepow, Irwin H.
Ratnoff, Oscar D.
Levy, Lawrence R.
author_facet Lepow, Irwin H.
Ratnoff, Oscar D.
Levy, Lawrence R.
author_sort Lepow, Irwin H.
collection PubMed
description It has been found that under a wide range of physico-chemical conditions a positive correlation exists between the rate of disappearance of hemolytically active, partially purified first component of human complement and the rate of activation of an esterase hydrolyzing N-acetyl-L-tyrosine ethyl ester. Both reactions follow the kinetic equation for second order autocatalysis, with an apparent energy of activation of 31,000 calories per mol. They occur optimally at pH 7.3–7.7 and are inhibited by ionic strengths greater than 0.15, by 5 x 10(5) M ethylenediaminetetraacetic acid, and by a heat-labile serum inhibitor which appears unrelated to any component of complement. The activation of first component to esterase resembles closely the activation of trypsinogen to trypsin. Partially purified first component, containing plasminogen, may also be activated to esterase by addition of streptokinase. The significance of these data with respect to the postulated existence of first component as a proesterase and its possible role in complement-"fixation" is discussed.
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spelling pubmed-21366872008-04-17 STUDIES ON THE ACTIVATION OF A PROESTERASE ASSOCIATED WITH PARTIALLY PURIFIED FIRST COMPONENT OF HUMAN COMPLEMENT Lepow, Irwin H. Ratnoff, Oscar D. Levy, Lawrence R. J Exp Med Article It has been found that under a wide range of physico-chemical conditions a positive correlation exists between the rate of disappearance of hemolytically active, partially purified first component of human complement and the rate of activation of an esterase hydrolyzing N-acetyl-L-tyrosine ethyl ester. Both reactions follow the kinetic equation for second order autocatalysis, with an apparent energy of activation of 31,000 calories per mol. They occur optimally at pH 7.3–7.7 and are inhibited by ionic strengths greater than 0.15, by 5 x 10(5) M ethylenediaminetetraacetic acid, and by a heat-labile serum inhibitor which appears unrelated to any component of complement. The activation of first component to esterase resembles closely the activation of trypsinogen to trypsin. Partially purified first component, containing plasminogen, may also be activated to esterase by addition of streptokinase. The significance of these data with respect to the postulated existence of first component as a proesterase and its possible role in complement-"fixation" is discussed. The Rockefeller University Press 1958-02-28 /pmc/articles/PMC2136687/ /pubmed/13513912 Text en Copyright © Copyright, 1958, by The Rockefeller Institute for Medical Research New York 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
Lepow, Irwin H.
Ratnoff, Oscar D.
Levy, Lawrence R.
STUDIES ON THE ACTIVATION OF A PROESTERASE ASSOCIATED WITH PARTIALLY PURIFIED FIRST COMPONENT OF HUMAN COMPLEMENT
title STUDIES ON THE ACTIVATION OF A PROESTERASE ASSOCIATED WITH PARTIALLY PURIFIED FIRST COMPONENT OF HUMAN COMPLEMENT
title_full STUDIES ON THE ACTIVATION OF A PROESTERASE ASSOCIATED WITH PARTIALLY PURIFIED FIRST COMPONENT OF HUMAN COMPLEMENT
title_fullStr STUDIES ON THE ACTIVATION OF A PROESTERASE ASSOCIATED WITH PARTIALLY PURIFIED FIRST COMPONENT OF HUMAN COMPLEMENT
title_full_unstemmed STUDIES ON THE ACTIVATION OF A PROESTERASE ASSOCIATED WITH PARTIALLY PURIFIED FIRST COMPONENT OF HUMAN COMPLEMENT
title_short STUDIES ON THE ACTIVATION OF A PROESTERASE ASSOCIATED WITH PARTIALLY PURIFIED FIRST COMPONENT OF HUMAN COMPLEMENT
title_sort studies on the activation of a proesterase associated with partially purified first component of human complement
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2136687/
https://www.ncbi.nlm.nih.gov/pubmed/13513912
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