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Variations of the Contractile Apparatus in Smooth and Striated Muscles : X-ray diffraction studies at rest and in contraction

Structural information is presented for three muscle systems—mammalian smooth muscle at rest and partially active, living toad striated muscle at rest and contracting, and glycerinated rabbit psoas muscle under various conditions of pH and ionic environment. In the smooth muscle no evidence of organ...

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Detalles Bibliográficos
Autor principal: Elliott, G. F.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1967
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225749/
https://www.ncbi.nlm.nih.gov/pubmed/6050595
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author Elliott, G. F.
author_facet Elliott, G. F.
author_sort Elliott, G. F.
collection PubMed
description Structural information is presented for three muscle systems—mammalian smooth muscle at rest and partially active, living toad striated muscle at rest and contracting, and glycerinated rabbit psoas muscle under various conditions of pH and ionic environment. In the smooth muscle no evidence of organized myosin filaments has been found. In the striated muscle the myosin-to-actin distance can vary widely, according to sarcomere length and to muscle treatment, both at rest and during contraction. In the discussion it is suggested that muscle should be considered as a colloidal system and that there need not necessarily be any chemical bonding (cross-linking) involved in the contractile process.
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spelling pubmed-22257492008-04-23 Variations of the Contractile Apparatus in Smooth and Striated Muscles : X-ray diffraction studies at rest and in contraction Elliott, G. F. J Gen Physiol Comparative Aspects of Muscular Contraction Structural information is presented for three muscle systems—mammalian smooth muscle at rest and partially active, living toad striated muscle at rest and contracting, and glycerinated rabbit psoas muscle under various conditions of pH and ionic environment. In the smooth muscle no evidence of organized myosin filaments has been found. In the striated muscle the myosin-to-actin distance can vary widely, according to sarcomere length and to muscle treatment, both at rest and during contraction. In the discussion it is suggested that muscle should be considered as a colloidal system and that there need not necessarily be any chemical bonding (cross-linking) involved in the contractile process. The Rockefeller University Press 1967-07-01 /pmc/articles/PMC2225749/ /pubmed/6050595 Text en Copyright © 1967 by The Rockefeller University Press 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 Comparative Aspects of Muscular Contraction
Elliott, G. F.
Variations of the Contractile Apparatus in Smooth and Striated Muscles : X-ray diffraction studies at rest and in contraction
title Variations of the Contractile Apparatus in Smooth and Striated Muscles : X-ray diffraction studies at rest and in contraction
title_full Variations of the Contractile Apparatus in Smooth and Striated Muscles : X-ray diffraction studies at rest and in contraction
title_fullStr Variations of the Contractile Apparatus in Smooth and Striated Muscles : X-ray diffraction studies at rest and in contraction
title_full_unstemmed Variations of the Contractile Apparatus in Smooth and Striated Muscles : X-ray diffraction studies at rest and in contraction
title_short Variations of the Contractile Apparatus in Smooth and Striated Muscles : X-ray diffraction studies at rest and in contraction
title_sort variations of the contractile apparatus in smooth and striated muscles : x-ray diffraction studies at rest and in contraction
topic Comparative Aspects of Muscular Contraction
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225749/
https://www.ncbi.nlm.nih.gov/pubmed/6050595
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