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AN ADENOSINETRIPHOSPHATE-ACTIVATED HEMOLYTIC SYSTEM

1. Hemolyzed rabbit cells contain a factor which lyses human erythrocytes in vitro when Mg(++) and certain nucleotides are supplied to the system. Of the nucleotides tested ATP is the most active, although no net loss of ATP or of labile phosphate seems to be associated with the hemolytic process. 2...

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Detalles Bibliográficos
Autores principales: Borek, Blanche Ann, Bovarnick, Max
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1956
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147610/
https://www.ncbi.nlm.nih.gov/pubmed/13357741
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author Borek, Blanche Ann
Bovarnick, Max
author_facet Borek, Blanche Ann
Bovarnick, Max
author_sort Borek, Blanche Ann
collection PubMed
description 1. Hemolyzed rabbit cells contain a factor which lyses human erythrocytes in vitro when Mg(++) and certain nucleotides are supplied to the system. Of the nucleotides tested ATP is the most active, although no net loss of ATP or of labile phosphate seems to be associated with the hemolytic process. 2. The lytic factor appears to be a sulfhydryl enzyme which attacks the membrane of the human red cell, its hemolytic activity being inhibited by human stroma. 3. The system is activated by glutathione and is inhibited by heavy metals, oxidized glutathione, cysteine, ergothionine, and a number of metabolic inhibitors. Physostigmine has no effect. 4. Partial purification of the lytic factor has been achieved by fractional centrifugation.
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spelling pubmed-21476102008-04-23 AN ADENOSINETRIPHOSPHATE-ACTIVATED HEMOLYTIC SYSTEM Borek, Blanche Ann Bovarnick, Max J Gen Physiol Article 1. Hemolyzed rabbit cells contain a factor which lyses human erythrocytes in vitro when Mg(++) and certain nucleotides are supplied to the system. Of the nucleotides tested ATP is the most active, although no net loss of ATP or of labile phosphate seems to be associated with the hemolytic process. 2. The lytic factor appears to be a sulfhydryl enzyme which attacks the membrane of the human red cell, its hemolytic activity being inhibited by human stroma. 3. The system is activated by glutathione and is inhibited by heavy metals, oxidized glutathione, cysteine, ergothionine, and a number of metabolic inhibitors. Physostigmine has no effect. 4. Partial purification of the lytic factor has been achieved by fractional centrifugation. The Rockefeller University Press 1956-09-20 /pmc/articles/PMC2147610/ /pubmed/13357741 Text en Copyright © Copyright, 1956, 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
Borek, Blanche Ann
Bovarnick, Max
AN ADENOSINETRIPHOSPHATE-ACTIVATED HEMOLYTIC SYSTEM
title AN ADENOSINETRIPHOSPHATE-ACTIVATED HEMOLYTIC SYSTEM
title_full AN ADENOSINETRIPHOSPHATE-ACTIVATED HEMOLYTIC SYSTEM
title_fullStr AN ADENOSINETRIPHOSPHATE-ACTIVATED HEMOLYTIC SYSTEM
title_full_unstemmed AN ADENOSINETRIPHOSPHATE-ACTIVATED HEMOLYTIC SYSTEM
title_short AN ADENOSINETRIPHOSPHATE-ACTIVATED HEMOLYTIC SYSTEM
title_sort adenosinetriphosphate-activated hemolytic system
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147610/
https://www.ncbi.nlm.nih.gov/pubmed/13357741
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