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THE INACTIVATION OF TRYPSIN : III. SPONTANEOUS INACTIVATION.
1. The rate of inactivation of purified trypsin solutions approximates closely that demanded by the monomolecular formula. The more carefully the solution is purified the closer the agreement with the formula. 2. The products formed by the action of trypsin on proteins renders the trypsin more stabl...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1922
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140503/ https://www.ncbi.nlm.nih.gov/pubmed/19871930 |
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author | Northrop, John H. |
author_facet | Northrop, John H. |
author_sort | Northrop, John H. |
collection | PubMed |
description | 1. The rate of inactivation of purified trypsin solutions approximates closely that demanded by the monomolecular formula. The more carefully the solution is purified the closer the agreement with the formula. 2. The products formed by the action of trypsin on proteins renders the trypsin more stable. Gelatin and glycine have no effect. 3. The rate of inactivation of trypsin solutions containing these products does not follow the course of a monomolecular reaction but becomes progressively slower than the predicted rate. 4. The protective action of these substances is much greater if they are added all at once at the beginning of the experiment than if they are added at intervals. These observations may be quantitatively accounted for by the hypothesis that a compound is formed between trypsin and the inhibiting substance which is stable as well as inactive, and that the rate of decomposition depends on the amount of uncombined trypsin present. 5. Trypsin is most stable at a pH of 5 and is rapidly destroyed in strongly acid or alkaline solution. 6. The protective effect of the inhibiting substances is small on the acid side of pH 5, increases from pH 5 to 7, and then remains approximately constant. |
format | Text |
id | pubmed-2140503 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1922 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21405032008-04-23 THE INACTIVATION OF TRYPSIN : III. SPONTANEOUS INACTIVATION. Northrop, John H. J Gen Physiol Article 1. The rate of inactivation of purified trypsin solutions approximates closely that demanded by the monomolecular formula. The more carefully the solution is purified the closer the agreement with the formula. 2. The products formed by the action of trypsin on proteins renders the trypsin more stable. Gelatin and glycine have no effect. 3. The rate of inactivation of trypsin solutions containing these products does not follow the course of a monomolecular reaction but becomes progressively slower than the predicted rate. 4. The protective action of these substances is much greater if they are added all at once at the beginning of the experiment than if they are added at intervals. These observations may be quantitatively accounted for by the hypothesis that a compound is formed between trypsin and the inhibiting substance which is stable as well as inactive, and that the rate of decomposition depends on the amount of uncombined trypsin present. 5. Trypsin is most stable at a pH of 5 and is rapidly destroyed in strongly acid or alkaline solution. 6. The protective effect of the inhibiting substances is small on the acid side of pH 5, increases from pH 5 to 7, and then remains approximately constant. The Rockefeller University Press 1922-01-20 /pmc/articles/PMC2140503/ /pubmed/19871930 Text en Copyright © Copyright, 1922, 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 Northrop, John H. THE INACTIVATION OF TRYPSIN : III. SPONTANEOUS INACTIVATION. |
title | THE INACTIVATION OF TRYPSIN : III. SPONTANEOUS INACTIVATION. |
title_full | THE INACTIVATION OF TRYPSIN : III. SPONTANEOUS INACTIVATION. |
title_fullStr | THE INACTIVATION OF TRYPSIN : III. SPONTANEOUS INACTIVATION. |
title_full_unstemmed | THE INACTIVATION OF TRYPSIN : III. SPONTANEOUS INACTIVATION. |
title_short | THE INACTIVATION OF TRYPSIN : III. SPONTANEOUS INACTIVATION. |
title_sort | inactivation of trypsin : iii. spontaneous inactivation. |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140503/ https://www.ncbi.nlm.nih.gov/pubmed/19871930 |
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