PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES : III. KINETICS OF THE HEAT INACTIVATION OF PAPAIN, BROMELIN, AND ASCLEPAIN

1. The rates of heat inactivation of papain, bromelin, and asclepain were determined at several different temperatures. Papain was by far the most resistant to heat. 2. The destruction of papain at 75–83° and bromelin at 55–70° followed the course of a first order reaction, except that for longer ti...

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Autores principales: Winnick, Theodore, Davis, Alva R., Greenberg, David M.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1940
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2237929/
https://www.ncbi.nlm.nih.gov/pubmed/19873156
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author Winnick, Theodore
Davis, Alva R.
Greenberg, David M.
author_facet Winnick, Theodore
Davis, Alva R.
Greenberg, David M.
author_sort Winnick, Theodore
collection PubMed
description 1. The rates of heat inactivation of papain, bromelin, and asclepain were determined at several different temperatures. Papain was by far the most resistant to heat. 2. The destruction of papain at 75–83° and bromelin at 55–70° followed the course of a first order reaction, except that for longer times of heating, bromelin (at 60–70°) was inactivated more rapidly than the first order equation required. 3. The rate of inactivation of asclepain at 55–70° followed the second order equation. 4. The critical thermal increments of inactivation of papain and bromelin, calculated with the van't Hoff-Arrhenius equation, were of the same high order that has been found for protein denaturation. The increment for asclepain was somewhat lower.
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spelling pubmed-22379292008-04-23 PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES : III. KINETICS OF THE HEAT INACTIVATION OF PAPAIN, BROMELIN, AND ASCLEPAIN Winnick, Theodore Davis, Alva R. Greenberg, David M. J Gen Physiol Article 1. The rates of heat inactivation of papain, bromelin, and asclepain were determined at several different temperatures. Papain was by far the most resistant to heat. 2. The destruction of papain at 75–83° and bromelin at 55–70° followed the course of a first order reaction, except that for longer times of heating, bromelin (at 60–70°) was inactivated more rapidly than the first order equation required. 3. The rate of inactivation of asclepain at 55–70° followed the second order equation. 4. The critical thermal increments of inactivation of papain and bromelin, calculated with the van't Hoff-Arrhenius equation, were of the same high order that has been found for protein denaturation. The increment for asclepain was somewhat lower. The Rockefeller University Press 1940-01-20 /pmc/articles/PMC2237929/ /pubmed/19873156 Text en Copyright © Copyright, 1940, 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
Winnick, Theodore
Davis, Alva R.
Greenberg, David M.
PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES : III. KINETICS OF THE HEAT INACTIVATION OF PAPAIN, BROMELIN, AND ASCLEPAIN
title PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES : III. KINETICS OF THE HEAT INACTIVATION OF PAPAIN, BROMELIN, AND ASCLEPAIN
title_full PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES : III. KINETICS OF THE HEAT INACTIVATION OF PAPAIN, BROMELIN, AND ASCLEPAIN
title_fullStr PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES : III. KINETICS OF THE HEAT INACTIVATION OF PAPAIN, BROMELIN, AND ASCLEPAIN
title_full_unstemmed PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES : III. KINETICS OF THE HEAT INACTIVATION OF PAPAIN, BROMELIN, AND ASCLEPAIN
title_short PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES : III. KINETICS OF THE HEAT INACTIVATION OF PAPAIN, BROMELIN, AND ASCLEPAIN
title_sort physicochemical properties of the proteolytic enzyme from the latex of the milkweed, asclepias speciosa torr. some comparisons with other proteases : iii. kinetics of the heat inactivation of papain, bromelin, and asclepain
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2237929/
https://www.ncbi.nlm.nih.gov/pubmed/19873156
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