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THE MECHANISM OF COMPLEMENT ACTION
It has been shown: 1. That complement exposed to ultra-violet light is not thereby sensitized to the action of heat (which indicates that it is not protein). 2. That inactivation of complement by ultra-violet light is accompanied by a decrease in its surface tension. 3. That photoinactivation of com...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1920
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140426/ https://www.ncbi.nlm.nih.gov/pubmed/19871856 |
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author | Brooks, S. C. |
author_facet | Brooks, S. C. |
author_sort | Brooks, S. C. |
collection | PubMed |
description | It has been shown: 1. That complement exposed to ultra-violet light is not thereby sensitized to the action of heat (which indicates that it is not protein). 2. That inactivation of complement by ultra-violet light is accompanied by a decrease in its surface tension. 3. That photoinactivation of complement is not a result of any changes in hydrogen ion concentration since these are less than 0.05 pH. 4. That hydrogen ion concentrations high enough to transform serum proteins from the cation to the anion condition (i.e. past the isoelectric point) permanently inactivate complement. These facts together with those given in previous papers lead to the following hypotheses. 1. That there is present in serum a hemolytic substance which is formed from a precursor (which may resemble lecithin) and is constantly being formed and simultaneously being broken down into inactive products. 2. That both precursor and lysin contain the same photosensitive molecular group. 3. That the lytic substance is dependent for its activity upon the state of the serum proteins. |
format | Text |
id | pubmed-2140426 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1920 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21404262008-04-23 THE MECHANISM OF COMPLEMENT ACTION Brooks, S. C. J Gen Physiol Article It has been shown: 1. That complement exposed to ultra-violet light is not thereby sensitized to the action of heat (which indicates that it is not protein). 2. That inactivation of complement by ultra-violet light is accompanied by a decrease in its surface tension. 3. That photoinactivation of complement is not a result of any changes in hydrogen ion concentration since these are less than 0.05 pH. 4. That hydrogen ion concentrations high enough to transform serum proteins from the cation to the anion condition (i.e. past the isoelectric point) permanently inactivate complement. These facts together with those given in previous papers lead to the following hypotheses. 1. That there is present in serum a hemolytic substance which is formed from a precursor (which may resemble lecithin) and is constantly being formed and simultaneously being broken down into inactive products. 2. That both precursor and lysin contain the same photosensitive molecular group. 3. That the lytic substance is dependent for its activity upon the state of the serum proteins. The Rockefeller University Press 1920-11-20 /pmc/articles/PMC2140426/ /pubmed/19871856 Text en Copyright © Copyright, 1920, by The Rockefeller Institute for Medical Research 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 Brooks, S. C. THE MECHANISM OF COMPLEMENT ACTION |
title | THE MECHANISM OF COMPLEMENT ACTION |
title_full | THE MECHANISM OF COMPLEMENT ACTION |
title_fullStr | THE MECHANISM OF COMPLEMENT ACTION |
title_full_unstemmed | THE MECHANISM OF COMPLEMENT ACTION |
title_short | THE MECHANISM OF COMPLEMENT ACTION |
title_sort | mechanism of complement action |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140426/ https://www.ncbi.nlm.nih.gov/pubmed/19871856 |
work_keys_str_mv | AT brookssc themechanismofcomplementaction AT brookssc mechanismofcomplementaction |