THE CHANGE IN STATE OF THE PROTEINS OF MUSCLE IN RIGOR

1. When myosin is exposed to a typical denaturing agent (acid) it becomes insoluble and its SH groups are activated. 2. The same number of active SH groups is found in the soluble myosin of resting muscle as in the insoluble myosin of muscle in rigor. No activation of SH groups accompanies the forma...

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Detalles Bibliográficos
Autor principal: Mirsky, A. E.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1936
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141461/
https://www.ncbi.nlm.nih.gov/pubmed/19872948
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author Mirsky, A. E.
author_facet Mirsky, A. E.
author_sort Mirsky, A. E.
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description 1. When myosin is exposed to a typical denaturing agent (acid) it becomes insoluble and its SH groups are activated. 2. The same number of active SH groups is found in the soluble myosin of resting muscle as in the insoluble myosin of muscle in rigor. No activation of SH groups accompanies the formation of insoluble protein in rigor. 3. When the insoluble myosin of muscle in rigor is treated with a denaturing agent its SH groups are activated. 4. Protein coagulation as brought about by denaturing agents (heat, acid, alkali, alcohol, urea, salicylate, surface forces, ultraviolet light) is a distinctly different change from the coagulation of myosin brought about by the unknown agent in muscle.
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spelling pubmed-21414612008-04-23 THE CHANGE IN STATE OF THE PROTEINS OF MUSCLE IN RIGOR Mirsky, A. E. J Gen Physiol Article 1. When myosin is exposed to a typical denaturing agent (acid) it becomes insoluble and its SH groups are activated. 2. The same number of active SH groups is found in the soluble myosin of resting muscle as in the insoluble myosin of muscle in rigor. No activation of SH groups accompanies the formation of insoluble protein in rigor. 3. When the insoluble myosin of muscle in rigor is treated with a denaturing agent its SH groups are activated. 4. Protein coagulation as brought about by denaturing agents (heat, acid, alkali, alcohol, urea, salicylate, surface forces, ultraviolet light) is a distinctly different change from the coagulation of myosin brought about by the unknown agent in muscle. The Rockefeller University Press 1936-03-20 /pmc/articles/PMC2141461/ /pubmed/19872948 Text en Copyright © Copyright, 1936, 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
Mirsky, A. E.
THE CHANGE IN STATE OF THE PROTEINS OF MUSCLE IN RIGOR
title THE CHANGE IN STATE OF THE PROTEINS OF MUSCLE IN RIGOR
title_full THE CHANGE IN STATE OF THE PROTEINS OF MUSCLE IN RIGOR
title_fullStr THE CHANGE IN STATE OF THE PROTEINS OF MUSCLE IN RIGOR
title_full_unstemmed THE CHANGE IN STATE OF THE PROTEINS OF MUSCLE IN RIGOR
title_short THE CHANGE IN STATE OF THE PROTEINS OF MUSCLE IN RIGOR
title_sort change in state of the proteins of muscle in rigor
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141461/
https://www.ncbi.nlm.nih.gov/pubmed/19872948
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