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PHAGE FORMATION IN STAPHYLOCOCCUS MUSCAE CULTURES : VII. PARTIAL PURIFICATION OF THE PROTEIN FACTOR NECESSARY FOR VIRUS SYNTHESIS

1. A substance is present in autolyzed pepsin solutions which stimulates the release of phage by some strains of S. muscae when added to Fildes' synthetic medium. 2. The substance is assayed by determining the quantity necessary to increase the phage yield to one-half the maximum value, using t...

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Detalles Bibliográficos
Autor principal: Price, Winston H.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1950
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147253/
https://www.ncbi.nlm.nih.gov/pubmed/14824493
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author Price, Winston H.
author_facet Price, Winston H.
author_sort Price, Winston H.
collection PubMed
description 1. A substance is present in autolyzed pepsin solutions which stimulates the release of phage by some strains of S. muscae when added to Fildes' synthetic medium. 2. The substance is assayed by determining the quantity necessary to increase the phage yield to one-half the maximum value, using the one-step growth curve technique. 3. The substance has been concentrated and partially purified (500-fold) by heavy metal precipitation, butyl alcohol extraction, and absorption on norit. 4. No known amino acid or accessory growth substance tested could replace this substance.
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spelling pubmed-21472532008-04-23 PHAGE FORMATION IN STAPHYLOCOCCUS MUSCAE CULTURES : VII. PARTIAL PURIFICATION OF THE PROTEIN FACTOR NECESSARY FOR VIRUS SYNTHESIS Price, Winston H. J Gen Physiol Article 1. A substance is present in autolyzed pepsin solutions which stimulates the release of phage by some strains of S. muscae when added to Fildes' synthetic medium. 2. The substance is assayed by determining the quantity necessary to increase the phage yield to one-half the maximum value, using the one-step growth curve technique. 3. The substance has been concentrated and partially purified (500-fold) by heavy metal precipitation, butyl alcohol extraction, and absorption on norit. 4. No known amino acid or accessory growth substance tested could replace this substance. The Rockefeller University Press 1950-11-20 /pmc/articles/PMC2147253/ /pubmed/14824493 Text en Copyright © Copyright, 1950, 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
Price, Winston H.
PHAGE FORMATION IN STAPHYLOCOCCUS MUSCAE CULTURES : VII. PARTIAL PURIFICATION OF THE PROTEIN FACTOR NECESSARY FOR VIRUS SYNTHESIS
title PHAGE FORMATION IN STAPHYLOCOCCUS MUSCAE CULTURES : VII. PARTIAL PURIFICATION OF THE PROTEIN FACTOR NECESSARY FOR VIRUS SYNTHESIS
title_full PHAGE FORMATION IN STAPHYLOCOCCUS MUSCAE CULTURES : VII. PARTIAL PURIFICATION OF THE PROTEIN FACTOR NECESSARY FOR VIRUS SYNTHESIS
title_fullStr PHAGE FORMATION IN STAPHYLOCOCCUS MUSCAE CULTURES : VII. PARTIAL PURIFICATION OF THE PROTEIN FACTOR NECESSARY FOR VIRUS SYNTHESIS
title_full_unstemmed PHAGE FORMATION IN STAPHYLOCOCCUS MUSCAE CULTURES : VII. PARTIAL PURIFICATION OF THE PROTEIN FACTOR NECESSARY FOR VIRUS SYNTHESIS
title_short PHAGE FORMATION IN STAPHYLOCOCCUS MUSCAE CULTURES : VII. PARTIAL PURIFICATION OF THE PROTEIN FACTOR NECESSARY FOR VIRUS SYNTHESIS
title_sort phage formation in staphylococcus muscae cultures : vii. partial purification of the protein factor necessary for virus synthesis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147253/
https://www.ncbi.nlm.nih.gov/pubmed/14824493
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