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STAPHYLOCOCCAL VIROLYSIN, A PHAGE-INDUCED LYSIN : ITS DIFFERENTIATION FROM THE AUTOLYSIN OF NORMAL CELLS
Virolysin is a lysin which appears in Staphylococcus aureus K(1) cells infected with phage P(14); together with phage, virolysin is released from phage-infected cells at the time of lysis. Autolysin is a lysin formed by uninfected cells of the K(1) strain; autolysin is released from uninfected cells...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1957
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147651/ https://www.ncbi.nlm.nih.gov/pubmed/13428989 |
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author | Ralston, D. J. Lieberman, Miriam Baer, B. Krueger, A. P. |
author_facet | Ralston, D. J. Lieberman, Miriam Baer, B. Krueger, A. P. |
author_sort | Ralston, D. J. |
collection | PubMed |
description | Virolysin is a lysin which appears in Staphylococcus aureus K(1) cells infected with phage P(14); together with phage, virolysin is released from phage-infected cells at the time of lysis. Autolysin is a lysin formed by uninfected cells of the K(1) strain; autolysin is released from uninfected cells by autolysis. They show the following similarities: Both agents act within the genus Micrococcus. They lyse cells only after the cell has been subjected to a damaging or "sensitizing" treatment, such as heat, bacteriophage, acetone, or ultraviolet irradiation. The course of lysis of heated cells by both lysins has been found to proceed in a similar manner. A constant percentage of cells is lysed, independent of the concentration of lysin; the residual cells remain resistant to either lysin. Lysis proceeds logarithmically with time, and the velocity constants K are proportional to the lysin concentration. K increases with increasing temperature. Both lysins are unaffected by antiserum to the phage. They are inhibited alike by a number of chemicals, including known enzyme inhibitors. Both agents are destroyed by proteolytic enzymes and are precipitated by 40 per cent saturation with (NH(4))(2)SO(4). Both lysins are very thermolabile. The two lysins differ with respect to their pH optimum, antigenic relationship and specificity for Micrococcus lysodeikticus. These results suggest that (1) both lysins have many properties associated with enzymes, (2) the lysis of heated cells, which they produce, has some of the characteristics of a chemical reaction, (3) the lysin from the phage-infected cell is clearly different from the lysin of the uninfected cell. |
format | Text |
id | pubmed-2147651 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1957 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21476512008-04-23 STAPHYLOCOCCAL VIROLYSIN, A PHAGE-INDUCED LYSIN : ITS DIFFERENTIATION FROM THE AUTOLYSIN OF NORMAL CELLS Ralston, D. J. Lieberman, Miriam Baer, B. Krueger, A. P. J Gen Physiol Article Virolysin is a lysin which appears in Staphylococcus aureus K(1) cells infected with phage P(14); together with phage, virolysin is released from phage-infected cells at the time of lysis. Autolysin is a lysin formed by uninfected cells of the K(1) strain; autolysin is released from uninfected cells by autolysis. They show the following similarities: Both agents act within the genus Micrococcus. They lyse cells only after the cell has been subjected to a damaging or "sensitizing" treatment, such as heat, bacteriophage, acetone, or ultraviolet irradiation. The course of lysis of heated cells by both lysins has been found to proceed in a similar manner. A constant percentage of cells is lysed, independent of the concentration of lysin; the residual cells remain resistant to either lysin. Lysis proceeds logarithmically with time, and the velocity constants K are proportional to the lysin concentration. K increases with increasing temperature. Both lysins are unaffected by antiserum to the phage. They are inhibited alike by a number of chemicals, including known enzyme inhibitors. Both agents are destroyed by proteolytic enzymes and are precipitated by 40 per cent saturation with (NH(4))(2)SO(4). Both lysins are very thermolabile. The two lysins differ with respect to their pH optimum, antigenic relationship and specificity for Micrococcus lysodeikticus. These results suggest that (1) both lysins have many properties associated with enzymes, (2) the lysis of heated cells, which they produce, has some of the characteristics of a chemical reaction, (3) the lysin from the phage-infected cell is clearly different from the lysin of the uninfected cell. The Rockefeller University Press 1957-05-20 /pmc/articles/PMC2147651/ /pubmed/13428989 Text en Copyright © Copyright, 1957, 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 Ralston, D. J. Lieberman, Miriam Baer, B. Krueger, A. P. STAPHYLOCOCCAL VIROLYSIN, A PHAGE-INDUCED LYSIN : ITS DIFFERENTIATION FROM THE AUTOLYSIN OF NORMAL CELLS |
title | STAPHYLOCOCCAL VIROLYSIN, A PHAGE-INDUCED LYSIN : ITS DIFFERENTIATION FROM THE AUTOLYSIN OF NORMAL CELLS |
title_full | STAPHYLOCOCCAL VIROLYSIN, A PHAGE-INDUCED LYSIN : ITS DIFFERENTIATION FROM THE AUTOLYSIN OF NORMAL CELLS |
title_fullStr | STAPHYLOCOCCAL VIROLYSIN, A PHAGE-INDUCED LYSIN : ITS DIFFERENTIATION FROM THE AUTOLYSIN OF NORMAL CELLS |
title_full_unstemmed | STAPHYLOCOCCAL VIROLYSIN, A PHAGE-INDUCED LYSIN : ITS DIFFERENTIATION FROM THE AUTOLYSIN OF NORMAL CELLS |
title_short | STAPHYLOCOCCAL VIROLYSIN, A PHAGE-INDUCED LYSIN : ITS DIFFERENTIATION FROM THE AUTOLYSIN OF NORMAL CELLS |
title_sort | staphylococcal virolysin, a phage-induced lysin : its differentiation from the autolysin of normal cells |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147651/ https://www.ncbi.nlm.nih.gov/pubmed/13428989 |
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