Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide.

In myofibrils, titin (also called connectin) molecules span from Z line to M line and constitute a third filament system containing an elastic domain in the I band. This giant protein is particularly sensitive to proteolysis in situ. Treatment of rabbit skeletal myofibrils with exogenous proteinases...

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Главные авторы: Astier, C, Labbé, J P, Roustan, C, Benyamin, Y
Формат: Статья
Язык:English
Опубликовано: 1993
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Research Article
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC1132341/
https://ncbi.nlm.nih.gov/pubmed/8457201
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spelling pubmed-11323412005-09-07 Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide. Astier, C Labbé, J P Roustan, C Benyamin, Y Biochem J Research Article In myofibrils, titin (also called connectin) molecules span from Z line to M line and constitute a third filament system containing an elastic domain in the I band. This giant protein is particularly sensitive to proteolysis in situ. Treatment of rabbit skeletal myofibrils with exogenous proteinases induces a release of titin fragments, which are detected in the soluble myofibrillar fraction. The cleavage of titin occurs at specific points localized at the proximity of Z line and could lead to a concomitant release of alpha-actinin. 1993-03-15 /pmc/articles/PMC1132341/ /pubmed/8457201 Text en
institution US National Library of Medicine
collection PubMed Central
language English
format Article
topic Research Article
spellingShingle Research Article
Astier, C
Labbé, J P
Roustan, C
Benyamin, Y
Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide.
description In myofibrils, titin (also called connectin) molecules span from Z line to M line and constitute a third filament system containing an elastic domain in the I band. This giant protein is particularly sensitive to proteolysis in situ. Treatment of rabbit skeletal myofibrils with exogenous proteinases induces a release of titin fragments, which are detected in the soluble myofibrillar fraction. The cleavage of titin occurs at specific points localized at the proximity of Z line and could lead to a concomitant release of alpha-actinin.
author Astier, C
Labbé, J P
Roustan, C
Benyamin, Y
author_facet Astier, C
Labbé, J P
Roustan, C
Benyamin, Y
author_sort Astier, C
title Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide.
title_short Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide.
title_full Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide.
title_fullStr Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide.
title_full_unstemmed Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide.
title_sort effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. purification of an 800 kda titin polypeptide.
publishDate 1993
url https://ncbi.nlm.nih.gov/pmc/articles/PMC1132341/
https://ncbi.nlm.nih.gov/pubmed/8457201
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