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 form...
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| Format: | Online |
| Language: | English |
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The Rockefeller University Press
1936
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141461/ |
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pubmed-2141461 |
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oai_dc |
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pubmed-21414612008-04-23 THE CHANGE IN STATE OF THE PROTEINS OF MUSCLE IN RIGOR Mirsky, A. E. 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/). |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Mirsky, A. E. |
| spellingShingle |
Mirsky, A. E. THE CHANGE IN STATE OF THE PROTEINS OF MUSCLE IN RIGOR |
| author_facet |
Mirsky, A. E. |
| author_sort |
Mirsky, A. E. |
| title |
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_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_sort |
change in state of the proteins of muscle in rigor |
| 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. |
| publisher |
The Rockefeller University Press |
| publishDate |
1936 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141461/ |
| _version_ |
1611422819943448576 |