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Paramyosin in invertebrate muscles. II. Content in relation to structure and function
By quantitative sodium dodecyl sulfate-polyacrylamide gel electrophoresis, paramyosin:myosin heavy chain molecular ratios were calculated for three molluscan muscles:Aequipecten striated adductor, Mercenaria opaque adductor, and Mytilus anterior byssus retractor; and four arthropodan muscles:Limulus...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1976
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2109719/ https://www.ncbi.nlm.nih.gov/pubmed/977650 |
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collection | PubMed |
description | By quantitative sodium dodecyl sulfate-polyacrylamide gel electrophoresis, paramyosin:myosin heavy chain molecular ratios were calculated for three molluscan muscles:Aequipecten striated adductor, Mercenaria opaque adductor, and Mytilus anterior byssus retractor; and four arthropodan muscles:Limulus telson, Homarus slow claw. Balanus scutal depressor, and Lethocerus air tube retractor. These ratios correlate positively with both thick filament dimensions and maximum active tension development in these tissues. The role of paramyosin in these muscles is discussed with respect to the following characteristics: force development, "catch," and extreme reversible changes in length. |
format | Text |
id | pubmed-2109719 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1976 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21097192008-05-01 Paramyosin in invertebrate muscles. II. Content in relation to structure and function J Cell Biol Articles By quantitative sodium dodecyl sulfate-polyacrylamide gel electrophoresis, paramyosin:myosin heavy chain molecular ratios were calculated for three molluscan muscles:Aequipecten striated adductor, Mercenaria opaque adductor, and Mytilus anterior byssus retractor; and four arthropodan muscles:Limulus telson, Homarus slow claw. Balanus scutal depressor, and Lethocerus air tube retractor. These ratios correlate positively with both thick filament dimensions and maximum active tension development in these tissues. The role of paramyosin in these muscles is discussed with respect to the following characteristics: force development, "catch," and extreme reversible changes in length. The Rockefeller University Press 1976-10-01 /pmc/articles/PMC2109719/ /pubmed/977650 Text en 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 | Articles Paramyosin in invertebrate muscles. II. Content in relation to structure and function |
title | Paramyosin in invertebrate muscles. II. Content in relation to structure and function |
title_full | Paramyosin in invertebrate muscles. II. Content in relation to structure and function |
title_fullStr | Paramyosin in invertebrate muscles. II. Content in relation to structure and function |
title_full_unstemmed | Paramyosin in invertebrate muscles. II. Content in relation to structure and function |
title_short | Paramyosin in invertebrate muscles. II. Content in relation to structure and function |
title_sort | paramyosin in invertebrate muscles. ii. content in relation to structure and function |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2109719/ https://www.ncbi.nlm.nih.gov/pubmed/977650 |