STUDIES ON THE ENZYMES OF PNEUMOCOCCUS : II. LIPOLYTIC ENZYMES: ESTERASE.

1. Pneumococci contain an intracellular enzyme of marked lipolytic activity as measured by the acid liberated by its action on tributyrin. 2. Enzyme-containing solutions may be prepared by dissolving pneumococci in bile, or by extraction by other means. 3. The optimum reaction for maximum activity o...

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Detalles Bibliográficos
Autores principales: Avery, O. T., Cullen, Glenn E.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1920
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2128285/
https://www.ncbi.nlm.nih.gov/pubmed/19868461
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author Avery, O. T.
Cullen, Glenn E.
author_facet Avery, O. T.
Cullen, Glenn E.
author_sort Avery, O. T.
collection PubMed
description 1. Pneumococci contain an intracellular enzyme of marked lipolytic activity as measured by the acid liberated by its action on tributyrin. 2. Enzyme-containing solutions may be prepared by dissolving pneumococci in bile, or by extraction by other means. 3. The optimum reaction for maximum activity of the endolipase is about pH 7.8, which coincides with the optimum hydrogen ion concentration for growth of pneumococci. 4. Heating the enzyme for 10 minutes at 70°C. destroys its activity. 5. Attenuation of virulence of pneumococcus had no measureable effect on enzyme activity. 6. The possible relation of the endolipase to the mechanism of bile solubility is discussed.
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spelling pubmed-21282852008-04-18 STUDIES ON THE ENZYMES OF PNEUMOCOCCUS : II. LIPOLYTIC ENZYMES: ESTERASE. Avery, O. T. Cullen, Glenn E. J Exp Med Article 1. Pneumococci contain an intracellular enzyme of marked lipolytic activity as measured by the acid liberated by its action on tributyrin. 2. Enzyme-containing solutions may be prepared by dissolving pneumococci in bile, or by extraction by other means. 3. The optimum reaction for maximum activity of the endolipase is about pH 7.8, which coincides with the optimum hydrogen ion concentration for growth of pneumococci. 4. Heating the enzyme for 10 minutes at 70°C. destroys its activity. 5. Attenuation of virulence of pneumococcus had no measureable effect on enzyme activity. 6. The possible relation of the endolipase to the mechanism of bile solubility is discussed. The Rockefeller University Press 1920-10-31 /pmc/articles/PMC2128285/ /pubmed/19868461 Text en Copyright © Copyright, 1920, by The Rockefeller Institute for Medical Research New York 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
Avery, O. T.
Cullen, Glenn E.
STUDIES ON THE ENZYMES OF PNEUMOCOCCUS : II. LIPOLYTIC ENZYMES: ESTERASE.
title STUDIES ON THE ENZYMES OF PNEUMOCOCCUS : II. LIPOLYTIC ENZYMES: ESTERASE.
title_full STUDIES ON THE ENZYMES OF PNEUMOCOCCUS : II. LIPOLYTIC ENZYMES: ESTERASE.
title_fullStr STUDIES ON THE ENZYMES OF PNEUMOCOCCUS : II. LIPOLYTIC ENZYMES: ESTERASE.
title_full_unstemmed STUDIES ON THE ENZYMES OF PNEUMOCOCCUS : II. LIPOLYTIC ENZYMES: ESTERASE.
title_short STUDIES ON THE ENZYMES OF PNEUMOCOCCUS : II. LIPOLYTIC ENZYMES: ESTERASE.
title_sort studies on the enzymes of pneumococcus : ii. lipolytic enzymes: esterase.
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2128285/
https://www.ncbi.nlm.nih.gov/pubmed/19868461
work_keys_str_mv AT averyot studiesontheenzymesofpneumococcusiilipolyticenzymesesterase
AT cullenglenne studiesontheenzymesofpneumococcusiilipolyticenzymesesterase

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