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THE PEPTASE, LIPASE, AND INVERTASE OF HEMOLYTIC STREPTOCOCCUS
1. A method has been outlined by which the enzymes of hemolytic streptococcus may be extracted with comparative ease. 2. The peptolytic enzyme is active between pH 4.4 and 8.7 with an optimum action at pH 7.2. It is destroyed in neutral phosphate solution at a temperature of 57°C. continued for 10 m...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1922
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2128322/ https://www.ncbi.nlm.nih.gov/pubmed/19868648 |
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author | Stevens, Franklin A. West, Randolph |
author_facet | Stevens, Franklin A. West, Randolph |
author_sort | Stevens, Franklin A. |
collection | PubMed |
description | 1. A method has been outlined by which the enzymes of hemolytic streptococcus may be extracted with comparative ease. 2. The peptolytic enzyme is active between pH 4.4 and 8.7 with an optimum action at pH 7.2. It is destroyed in neutral phosphate solution at a temperature of 57°C. continued for 10 minutes and at pH 5.0 deteriorates slowly at 37°C. Concentration experiments with solutions of the enzyme have shown that it resembles other enzymes. It is exceedingly susceptible to chloroform and its action is inhibited by dilutions of gentian violet. Casein is attacked but serum albumin is not digested after 3 days at 37°C. 3. The invertase is active between approximately pH 5.0 and 8.0 with an optimum of pH 7.0. It is destroyed by a temperature of 52°C. continued 10 minutes at an acid concentration of pH 7.0, or after 6 hours at 37°C. at pH 5.0. At this acidity it is more susceptible to heat than the peptase. 4. The lipase is active above pH 5.6. The greatest activity was observed at pH 7.9. It is completely destroyed after heating to temperatures over 55°C. for 10 minutes and resembles the invertase in its susceptibility to acid. |
format | Text |
id | pubmed-2128322 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1922 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21283222008-04-18 THE PEPTASE, LIPASE, AND INVERTASE OF HEMOLYTIC STREPTOCOCCUS Stevens, Franklin A. West, Randolph J Exp Med Article 1. A method has been outlined by which the enzymes of hemolytic streptococcus may be extracted with comparative ease. 2. The peptolytic enzyme is active between pH 4.4 and 8.7 with an optimum action at pH 7.2. It is destroyed in neutral phosphate solution at a temperature of 57°C. continued for 10 minutes and at pH 5.0 deteriorates slowly at 37°C. Concentration experiments with solutions of the enzyme have shown that it resembles other enzymes. It is exceedingly susceptible to chloroform and its action is inhibited by dilutions of gentian violet. Casein is attacked but serum albumin is not digested after 3 days at 37°C. 3. The invertase is active between approximately pH 5.0 and 8.0 with an optimum of pH 7.0. It is destroyed by a temperature of 52°C. continued 10 minutes at an acid concentration of pH 7.0, or after 6 hours at 37°C. at pH 5.0. At this acidity it is more susceptible to heat than the peptase. 4. The lipase is active above pH 5.6. The greatest activity was observed at pH 7.9. It is completely destroyed after heating to temperatures over 55°C. for 10 minutes and resembles the invertase in its susceptibility to acid. The Rockefeller University Press 1922-05-31 /pmc/articles/PMC2128322/ /pubmed/19868648 Text en Copyright © Copyright, 1922, 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 Stevens, Franklin A. West, Randolph THE PEPTASE, LIPASE, AND INVERTASE OF HEMOLYTIC STREPTOCOCCUS |
title | THE PEPTASE, LIPASE, AND INVERTASE OF HEMOLYTIC STREPTOCOCCUS |
title_full | THE PEPTASE, LIPASE, AND INVERTASE OF HEMOLYTIC STREPTOCOCCUS |
title_fullStr | THE PEPTASE, LIPASE, AND INVERTASE OF HEMOLYTIC STREPTOCOCCUS |
title_full_unstemmed | THE PEPTASE, LIPASE, AND INVERTASE OF HEMOLYTIC STREPTOCOCCUS |
title_short | THE PEPTASE, LIPASE, AND INVERTASE OF HEMOLYTIC STREPTOCOCCUS |
title_sort | peptase, lipase, and invertase of hemolytic streptococcus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2128322/ https://www.ncbi.nlm.nih.gov/pubmed/19868648 |
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