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M BAND PROTEIN : Two Components Isolated from Chicken Breast Muscle

M band protein can be specifically extracted from fresh chicken breast muscle myofibrils suspended in 5 mM Tris-HCl pH 8.0. During discontinuous polyacrylamide gel electrophoresis the isolated protein separates into three bands which can be identified as two separate components (A, B) and a complex...

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Detalles Bibliográficos
Autores principales: Eaton, Barbra L., Pepe, Frank A.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1972
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2108813/
https://www.ncbi.nlm.nih.gov/pubmed/4632583
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author Eaton, Barbra L.
Pepe, Frank A.
author_facet Eaton, Barbra L.
Pepe, Frank A.
author_sort Eaton, Barbra L.
collection PubMed
description M band protein can be specifically extracted from fresh chicken breast muscle myofibrils suspended in 5 mM Tris-HCl pH 8.0. During discontinuous polyacrylamide gel electrophoresis the isolated protein separates into three bands which can be identified as two separate components (A, B) and a complex of the two. When partially purified fractions of the separated components are combined, an increase in the intensity of the band containing the complex can be shown. The polypeptide chain weights of the two components are 100,000 (A) and 40,000 (B) daltons as estimated by sodium dodecyl sulfate- (SDS-) polyacrylamide gel electrophoresis. Antibody prepared against total M band protein stains only the M band of the myofibril and is completely absorbed by M band protein. M band protein also absorbs the M band staining specifically from antibody which stains both I and M bands. Immunodiffusion data indicate that anti-M band is a mixture of two specific antibodies, one against each component.
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spelling pubmed-21088132008-05-01 M BAND PROTEIN : Two Components Isolated from Chicken Breast Muscle Eaton, Barbra L. Pepe, Frank A. J Cell Biol Article M band protein can be specifically extracted from fresh chicken breast muscle myofibrils suspended in 5 mM Tris-HCl pH 8.0. During discontinuous polyacrylamide gel electrophoresis the isolated protein separates into three bands which can be identified as two separate components (A, B) and a complex of the two. When partially purified fractions of the separated components are combined, an increase in the intensity of the band containing the complex can be shown. The polypeptide chain weights of the two components are 100,000 (A) and 40,000 (B) daltons as estimated by sodium dodecyl sulfate- (SDS-) polyacrylamide gel electrophoresis. Antibody prepared against total M band protein stains only the M band of the myofibril and is completely absorbed by M band protein. M band protein also absorbs the M band staining specifically from antibody which stains both I and M bands. Immunodiffusion data indicate that anti-M band is a mixture of two specific antibodies, one against each component. The Rockefeller University Press 1972-12-01 /pmc/articles/PMC2108813/ /pubmed/4632583 Text en Copyright © 1972 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 Article
Eaton, Barbra L.
Pepe, Frank A.
M BAND PROTEIN : Two Components Isolated from Chicken Breast Muscle
title M BAND PROTEIN : Two Components Isolated from Chicken Breast Muscle
title_full M BAND PROTEIN : Two Components Isolated from Chicken Breast Muscle
title_fullStr M BAND PROTEIN : Two Components Isolated from Chicken Breast Muscle
title_full_unstemmed M BAND PROTEIN : Two Components Isolated from Chicken Breast Muscle
title_short M BAND PROTEIN : Two Components Isolated from Chicken Breast Muscle
title_sort m band protein : two components isolated from chicken breast muscle
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2108813/
https://www.ncbi.nlm.nih.gov/pubmed/4632583
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