Cargando…
STUDIES ON THE ANOMALOUS VISCOSITY AND FLOW-BIREFRINGENCE OF PROTEIN SOLUTIONS : III. CHANGES IN THESE PROPERTIES OF MYOSIN SOLUTIONS IN RELATION TO ADENOSINETRIPHOSPHATE AND MUSCULAR CONTRACTION
1. An investigation of the physicochemical properties of myosin has been carried out. Prepared under standard conditions, the ratio of flow-birefringence to protein concentration is uniform. The effect of electrolytes, pH, and urea on the flow-birefringence and viscosity (relative and anomalous) of...
Autores principales: | , , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1944
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2238015/ https://www.ncbi.nlm.nih.gov/pubmed/19873391 |
_version_ | 1782150442086563840 |
---|---|
author | Dainty, Mary Kleinzeller, Arnost Lawrence, A. S. C. Miall, Margaret Needham, Joseph Needham, Dorothy M. Shen, Shih-Chang |
author_facet | Dainty, Mary Kleinzeller, Arnost Lawrence, A. S. C. Miall, Margaret Needham, Joseph Needham, Dorothy M. Shen, Shih-Chang |
author_sort | Dainty, Mary |
collection | PubMed |
description | 1. An investigation of the physicochemical properties of myosin has been carried out. Prepared under standard conditions, the ratio of flow-birefringence to protein concentration is uniform. The effect of electrolytes, pH, and urea on the flow-birefringence and viscosity (relative and anomalous) of myosin has been examined. 2. Decrease or abolition of flow-birefringence does not necessarily imply far reaching denaturation, since such effects can be reversed by a variety of means. 3. When a myosin solution is treated with adenosinetriphosphate, its flow-birefringence is decreased (average 48 per cent), its anomalous viscosity is retained, and its relative viscosity is decreased (average 14 per cent). The full effect of adenosinetriphosphate is obtained at 0.004 M; a molarity very much less than that of other substances which decrease the flow-birefringence of myosin. 4. The changes in the physicochemical properties of myosin brought about by adenosinetriphosphate are spontaneously reversible, and are connected with the enzymatic action of the protein as adenosinetriphosphatase. 5. Effects similar to those of adenosinetriphosphate on the physicochemical properties of purified myosin have been obtained so far only with inosinetriphosphate. 6. Inorganic phosphate is split off by myosin from inosinetriphosphate as well as from adenosinetriphosphate. Inorganic triphosphate is split by 1 to 2 per cent solution of three times precipitated myosin. 7. Adenosinediphosphate and inorganic triphosphate act as competitive inhibitors with adenosinetriphosphate, blocking the fall of flow-birefringence. 8. The implications of the results, and the conception of active enzymic groups attached to proteins participating in cell structure, whether contractile or non-contractile, are discussed in relation to present views on muscle physiology and other biological problems. |
format | Text |
id | pubmed-2238015 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1944 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22380152008-04-23 STUDIES ON THE ANOMALOUS VISCOSITY AND FLOW-BIREFRINGENCE OF PROTEIN SOLUTIONS : III. CHANGES IN THESE PROPERTIES OF MYOSIN SOLUTIONS IN RELATION TO ADENOSINETRIPHOSPHATE AND MUSCULAR CONTRACTION Dainty, Mary Kleinzeller, Arnost Lawrence, A. S. C. Miall, Margaret Needham, Joseph Needham, Dorothy M. Shen, Shih-Chang J Gen Physiol Article 1. An investigation of the physicochemical properties of myosin has been carried out. Prepared under standard conditions, the ratio of flow-birefringence to protein concentration is uniform. The effect of electrolytes, pH, and urea on the flow-birefringence and viscosity (relative and anomalous) of myosin has been examined. 2. Decrease or abolition of flow-birefringence does not necessarily imply far reaching denaturation, since such effects can be reversed by a variety of means. 3. When a myosin solution is treated with adenosinetriphosphate, its flow-birefringence is decreased (average 48 per cent), its anomalous viscosity is retained, and its relative viscosity is decreased (average 14 per cent). The full effect of adenosinetriphosphate is obtained at 0.004 M; a molarity very much less than that of other substances which decrease the flow-birefringence of myosin. 4. The changes in the physicochemical properties of myosin brought about by adenosinetriphosphate are spontaneously reversible, and are connected with the enzymatic action of the protein as adenosinetriphosphatase. 5. Effects similar to those of adenosinetriphosphate on the physicochemical properties of purified myosin have been obtained so far only with inosinetriphosphate. 6. Inorganic phosphate is split off by myosin from inosinetriphosphate as well as from adenosinetriphosphate. Inorganic triphosphate is split by 1 to 2 per cent solution of three times precipitated myosin. 7. Adenosinediphosphate and inorganic triphosphate act as competitive inhibitors with adenosinetriphosphate, blocking the fall of flow-birefringence. 8. The implications of the results, and the conception of active enzymic groups attached to proteins participating in cell structure, whether contractile or non-contractile, are discussed in relation to present views on muscle physiology and other biological problems. The Rockefeller University Press 1944-03-20 /pmc/articles/PMC2238015/ /pubmed/19873391 Text en Copyright © Copyright, 1944, 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 Dainty, Mary Kleinzeller, Arnost Lawrence, A. S. C. Miall, Margaret Needham, Joseph Needham, Dorothy M. Shen, Shih-Chang STUDIES ON THE ANOMALOUS VISCOSITY AND FLOW-BIREFRINGENCE OF PROTEIN SOLUTIONS : III. CHANGES IN THESE PROPERTIES OF MYOSIN SOLUTIONS IN RELATION TO ADENOSINETRIPHOSPHATE AND MUSCULAR CONTRACTION |
title | STUDIES ON THE ANOMALOUS VISCOSITY AND FLOW-BIREFRINGENCE OF PROTEIN SOLUTIONS : III. CHANGES IN THESE PROPERTIES OF MYOSIN SOLUTIONS IN RELATION TO ADENOSINETRIPHOSPHATE AND MUSCULAR CONTRACTION |
title_full | STUDIES ON THE ANOMALOUS VISCOSITY AND FLOW-BIREFRINGENCE OF PROTEIN SOLUTIONS : III. CHANGES IN THESE PROPERTIES OF MYOSIN SOLUTIONS IN RELATION TO ADENOSINETRIPHOSPHATE AND MUSCULAR CONTRACTION |
title_fullStr | STUDIES ON THE ANOMALOUS VISCOSITY AND FLOW-BIREFRINGENCE OF PROTEIN SOLUTIONS : III. CHANGES IN THESE PROPERTIES OF MYOSIN SOLUTIONS IN RELATION TO ADENOSINETRIPHOSPHATE AND MUSCULAR CONTRACTION |
title_full_unstemmed | STUDIES ON THE ANOMALOUS VISCOSITY AND FLOW-BIREFRINGENCE OF PROTEIN SOLUTIONS : III. CHANGES IN THESE PROPERTIES OF MYOSIN SOLUTIONS IN RELATION TO ADENOSINETRIPHOSPHATE AND MUSCULAR CONTRACTION |
title_short | STUDIES ON THE ANOMALOUS VISCOSITY AND FLOW-BIREFRINGENCE OF PROTEIN SOLUTIONS : III. CHANGES IN THESE PROPERTIES OF MYOSIN SOLUTIONS IN RELATION TO ADENOSINETRIPHOSPHATE AND MUSCULAR CONTRACTION |
title_sort | studies on the anomalous viscosity and flow-birefringence of protein solutions : iii. changes in these properties of myosin solutions in relation to adenosinetriphosphate and muscular contraction |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2238015/ https://www.ncbi.nlm.nih.gov/pubmed/19873391 |
work_keys_str_mv | AT daintymary studiesontheanomalousviscosityandflowbirefringenceofproteinsolutionsiiichangesinthesepropertiesofmyosinsolutionsinrelationtoadenosinetriphosphateandmuscularcontraction AT kleinzellerarnost studiesontheanomalousviscosityandflowbirefringenceofproteinsolutionsiiichangesinthesepropertiesofmyosinsolutionsinrelationtoadenosinetriphosphateandmuscularcontraction AT lawrenceasc studiesontheanomalousviscosityandflowbirefringenceofproteinsolutionsiiichangesinthesepropertiesofmyosinsolutionsinrelationtoadenosinetriphosphateandmuscularcontraction AT miallmargaret studiesontheanomalousviscosityandflowbirefringenceofproteinsolutionsiiichangesinthesepropertiesofmyosinsolutionsinrelationtoadenosinetriphosphateandmuscularcontraction AT needhamjoseph studiesontheanomalousviscosityandflowbirefringenceofproteinsolutionsiiichangesinthesepropertiesofmyosinsolutionsinrelationtoadenosinetriphosphateandmuscularcontraction AT needhamdorothym studiesontheanomalousviscosityandflowbirefringenceofproteinsolutionsiiichangesinthesepropertiesofmyosinsolutionsinrelationtoadenosinetriphosphateandmuscularcontraction AT shenshihchang studiesontheanomalousviscosityandflowbirefringenceofproteinsolutionsiiichangesinthesepropertiesofmyosinsolutionsinrelationtoadenosinetriphosphateandmuscularcontraction |