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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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Detalles Bibliográficos
Autores principales: Emmart, E. W., Longley, J. B.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1954
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.
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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
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