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THE REACTIVATION OF HEAT-INACTIVATED HYALURONIDASE
1. Following heat denaturation after an hour at boiling temperature bovine testicular hyaluronidase has been shown to undergo spontaneous reactivation. 2. This reactivation is a function of the temperature at which the enzyme solution is maintained. 3. Secondary inactivation was observed to follow a...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1954
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147453/ https://www.ncbi.nlm.nih.gov/pubmed/13118106 |
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author | Emmart, E. W. Longley, J. B. |
author_facet | Emmart, E. W. Longley, J. B. |
author_sort | Emmart, E. W. |
collection | PubMed |
description | 1. Following heat denaturation after an hour at boiling temperature bovine testicular hyaluronidase has been shown to undergo spontaneous reactivation. 2. This reactivation is a function of the temperature at which the enzyme solution is maintained. 3. Secondary inactivation was observed to follow a reactivation of the enzyme at all concentrations observed. 4. There is a relationship between hydrolysis by the enzyme and the purity of the substrate. The demonstration of activity of the freshly boiled enzyme by the turbidimetric reduction technique is dependent upon the purity of the substrate. 5. These reactions have been demonstrated using preparations of bovine and avian hyaluronic acid and porcine chondroitin sulfate. |
format | Text |
id | pubmed-2147453 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1954 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21474532008-04-23 THE REACTIVATION OF HEAT-INACTIVATED HYALURONIDASE Emmart, E. W. Longley, J. B. J Gen Physiol Article 1. Following heat denaturation after an hour at boiling temperature bovine testicular hyaluronidase has been shown to undergo spontaneous reactivation. 2. This reactivation is a function of the temperature at which the enzyme solution is maintained. 3. Secondary inactivation was observed to follow a reactivation of the enzyme at all concentrations observed. 4. There is a relationship between hydrolysis by the enzyme and the purity of the substrate. The demonstration of activity of the freshly boiled enzyme by the turbidimetric reduction technique is dependent upon the purity of the substrate. 5. These reactions have been demonstrated using preparations of bovine and avian hyaluronic acid and porcine chondroitin sulfate. The Rockefeller University Press 1954-01-20 /pmc/articles/PMC2147453/ /pubmed/13118106 Text en Copyright © Copyright, 1954, 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 Emmart, E. W. Longley, J. B. THE REACTIVATION OF HEAT-INACTIVATED HYALURONIDASE |
title | THE REACTIVATION OF HEAT-INACTIVATED HYALURONIDASE |
title_full | THE REACTIVATION OF HEAT-INACTIVATED HYALURONIDASE |
title_fullStr | THE REACTIVATION OF HEAT-INACTIVATED HYALURONIDASE |
title_full_unstemmed | THE REACTIVATION OF HEAT-INACTIVATED HYALURONIDASE |
title_short | THE REACTIVATION OF HEAT-INACTIVATED HYALURONIDASE |
title_sort | reactivation of heat-inactivated hyaluronidase |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147453/ https://www.ncbi.nlm.nih.gov/pubmed/13118106 |
work_keys_str_mv | AT emmartew thereactivationofheatinactivatedhyaluronidase AT longleyjb thereactivationofheatinactivatedhyaluronidase AT emmartew reactivationofheatinactivatedhyaluronidase AT longleyjb reactivationofheatinactivatedhyaluronidase |