The Z-band: 85,000-dalton amorphin and alpha-actinin and their relation to structure

The conclusions arrived at as a result of this work can be summarized as follows: (a) We have found that there is an 85,000-dalton protein, which we have called 85K amorphin, associated with the Z-band of chicken pectoralis muscle myofibrils. We have isolated and purified this protein. It is not a s...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1982
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Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112221/
https://www.ncbi.nlm.nih.gov/pubmed/7130272
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collection PubMed
description The conclusions arrived at as a result of this work can be summarized as follows: (a) We have found that there is an 85,000-dalton protein, which we have called 85K amorphin, associated with the Z-band of chicken pectoralis muscle myofibrils. We have isolated and purified this protein. It is not a structural component of the Z-filaments since it can be extracted completely without extraction of the Z-filaments. Extraction of 85K amorphin results in loss of specific staining of the Z-band with fluorescence specific anti-85K amorphin. (b) We have found that alpha-actinin is the structural component of the Z-filaments, since extraction of alpha-actinin is accompanied by loss of the Z- filament structure.
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spelling pubmed-21122212008-05-01 The Z-band: 85,000-dalton amorphin and alpha-actinin and their relation to structure J Cell Biol Articles The conclusions arrived at as a result of this work can be summarized as follows: (a) We have found that there is an 85,000-dalton protein, which we have called 85K amorphin, associated with the Z-band of chicken pectoralis muscle myofibrils. We have isolated and purified this protein. It is not a structural component of the Z-filaments since it can be extracted completely without extraction of the Z-filaments. Extraction of 85K amorphin results in loss of specific staining of the Z-band with fluorescence specific anti-85K amorphin. (b) We have found that alpha-actinin is the structural component of the Z-filaments, since extraction of alpha-actinin is accompanied by loss of the Z- filament structure. The Rockefeller University Press 1982-09-01 /pmc/articles/PMC2112221/ /pubmed/7130272 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
The Z-band: 85,000-dalton amorphin and alpha-actinin and their relation to structure
title The Z-band: 85,000-dalton amorphin and alpha-actinin and their relation to structure
title_full The Z-band: 85,000-dalton amorphin and alpha-actinin and their relation to structure
title_fullStr The Z-band: 85,000-dalton amorphin and alpha-actinin and their relation to structure
title_full_unstemmed The Z-band: 85,000-dalton amorphin and alpha-actinin and their relation to structure
title_short The Z-band: 85,000-dalton amorphin and alpha-actinin and their relation to structure
title_sort z-band: 85,000-dalton amorphin and alpha-actinin and their relation to structure
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112221/
https://www.ncbi.nlm.nih.gov/pubmed/7130272

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