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OXYGEN-STABLE HEMOLYSINS OF GROUP A STREPTOCOCCI : IV. STUDIES ON THE MECHANISM OF LYSIS BY CELL-BOUND HEMOLYSIN OF RED BLOOD CELLS AND EHRLICH ASCITES TUMOR CELLS

In studies of the mechanism of lysis of red blood cells by washed streptococci with hemolytic activity (cell-bound hemolysin, CBH) no components released spontaneously by RBC or streptococci, or by interaction between these cells, could be found to induce the formation of soluble hemolysin by the st...

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Detalles Bibliográficos
Autores principales: Ginsburg, Isaac, Harris, T. N.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1965
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2137984/
https://www.ncbi.nlm.nih.gov/pubmed/14276781
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author Ginsburg, Isaac
Harris, T. N.
author_facet Ginsburg, Isaac
Harris, T. N.
author_sort Ginsburg, Isaac
collection PubMed
description In studies of the mechanism of lysis of red blood cells by washed streptococci with hemolytic activity (cell-bound hemolysin, CBH) no components released spontaneously by RBC or streptococci, or by interaction between these cells, could be found to induce the formation of soluble hemolysin by the streptococci. It was also found that separation of RBC from streptococci even by Millipore filter or a very thin layer of agar could prevent their hemolysis. By means of cellulose columns it was possible to separate RBC from streptococci after a short incubation. RBC thus separated from streptococci with which they had been incubated underwent hemolysis on subsequent incubation at 37°C. By varying the period of incubation prior to separation it was possible to demonstrate the transfer of increasing amounts of hemolysin from streptococci to RBC with increasing periods of incubation. A considerable part of this appeared to be at a constant rate. A theory is presented on the relationship between the streptococcal cell-bound hemolysin and the group of oxygen-stable streptococcal hemolysins, in terms of a transferable hemolytic moiety and binding sites for this moiety on the streptococcal cell, on various molecular species which can act as inducers of the oxygen-stable hemolysins, and on the RBC, with the affinity of the respective binding sites for the hemolytic moiety increasing in that order.
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spelling pubmed-21379842008-04-17 OXYGEN-STABLE HEMOLYSINS OF GROUP A STREPTOCOCCI : IV. STUDIES ON THE MECHANISM OF LYSIS BY CELL-BOUND HEMOLYSIN OF RED BLOOD CELLS AND EHRLICH ASCITES TUMOR CELLS Ginsburg, Isaac Harris, T. N. J Exp Med Article In studies of the mechanism of lysis of red blood cells by washed streptococci with hemolytic activity (cell-bound hemolysin, CBH) no components released spontaneously by RBC or streptococci, or by interaction between these cells, could be found to induce the formation of soluble hemolysin by the streptococci. It was also found that separation of RBC from streptococci even by Millipore filter or a very thin layer of agar could prevent their hemolysis. By means of cellulose columns it was possible to separate RBC from streptococci after a short incubation. RBC thus separated from streptococci with which they had been incubated underwent hemolysis on subsequent incubation at 37°C. By varying the period of incubation prior to separation it was possible to demonstrate the transfer of increasing amounts of hemolysin from streptococci to RBC with increasing periods of incubation. A considerable part of this appeared to be at a constant rate. A theory is presented on the relationship between the streptococcal cell-bound hemolysin and the group of oxygen-stable streptococcal hemolysins, in terms of a transferable hemolytic moiety and binding sites for this moiety on the streptococcal cell, on various molecular species which can act as inducers of the oxygen-stable hemolysins, and on the RBC, with the affinity of the respective binding sites for the hemolytic moiety increasing in that order. The Rockefeller University Press 1965-03-31 /pmc/articles/PMC2137984/ /pubmed/14276781 Text en Copyright © 1965 by The Rockefeller Institute 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
Ginsburg, Isaac
Harris, T. N.
OXYGEN-STABLE HEMOLYSINS OF GROUP A STREPTOCOCCI : IV. STUDIES ON THE MECHANISM OF LYSIS BY CELL-BOUND HEMOLYSIN OF RED BLOOD CELLS AND EHRLICH ASCITES TUMOR CELLS
title OXYGEN-STABLE HEMOLYSINS OF GROUP A STREPTOCOCCI : IV. STUDIES ON THE MECHANISM OF LYSIS BY CELL-BOUND HEMOLYSIN OF RED BLOOD CELLS AND EHRLICH ASCITES TUMOR CELLS
title_full OXYGEN-STABLE HEMOLYSINS OF GROUP A STREPTOCOCCI : IV. STUDIES ON THE MECHANISM OF LYSIS BY CELL-BOUND HEMOLYSIN OF RED BLOOD CELLS AND EHRLICH ASCITES TUMOR CELLS
title_fullStr OXYGEN-STABLE HEMOLYSINS OF GROUP A STREPTOCOCCI : IV. STUDIES ON THE MECHANISM OF LYSIS BY CELL-BOUND HEMOLYSIN OF RED BLOOD CELLS AND EHRLICH ASCITES TUMOR CELLS
title_full_unstemmed OXYGEN-STABLE HEMOLYSINS OF GROUP A STREPTOCOCCI : IV. STUDIES ON THE MECHANISM OF LYSIS BY CELL-BOUND HEMOLYSIN OF RED BLOOD CELLS AND EHRLICH ASCITES TUMOR CELLS
title_short OXYGEN-STABLE HEMOLYSINS OF GROUP A STREPTOCOCCI : IV. STUDIES ON THE MECHANISM OF LYSIS BY CELL-BOUND HEMOLYSIN OF RED BLOOD CELLS AND EHRLICH ASCITES TUMOR CELLS
title_sort oxygen-stable hemolysins of group a streptococci : iv. studies on the mechanism of lysis by cell-bound hemolysin of red blood cells and ehrlich ascites tumor cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2137984/
https://www.ncbi.nlm.nih.gov/pubmed/14276781
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