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Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from neurospora crassa mitochondria

Light-membrane fractions obtained by hypoosmotic lysis of neurospora crassa mitochondria exhibit buoyant densities and marker-enzyme activities characteristic of outer mitochondrial membranes. SDS PAGE of these membrane fractions indicates that a polypeptide of M(r) 31,000 is the main protein compon...

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Detalles Bibliográficos
Autor principal: Mannella, CA
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1982
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112230/
https://www.ncbi.nlm.nih.gov/pubmed/6215413
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author Mannella, CA
author_facet Mannella, CA
author_sort Mannella, CA
collection PubMed
description Light-membrane fractions obtained by hypoosmotic lysis of neurospora crassa mitochondria exhibit buoyant densities and marker-enzyme activities characteristic of outer mitochondrial membranes. SDS PAGE of these membrane fractions indicates that a polypeptide of M(r) 31,000 is the main protein component. Under negative-stain electron microscope examination many of the membranes in these fractions appear as large (0.5-1- mum diameter), collapsed vesicles. The surfaces of flattened, open (i.e., ripped) vesicles often exhibit extended two-dimensional arrays of subunits are arranged into hexagons within each parallelogram unit cell, 12.6x11.1 nm (lattice angle = 109 degrees).
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spelling pubmed-21122302008-05-01 Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from neurospora crassa mitochondria Mannella, CA J Cell Biol Articles Light-membrane fractions obtained by hypoosmotic lysis of neurospora crassa mitochondria exhibit buoyant densities and marker-enzyme activities characteristic of outer mitochondrial membranes. SDS PAGE of these membrane fractions indicates that a polypeptide of M(r) 31,000 is the main protein component. Under negative-stain electron microscope examination many of the membranes in these fractions appear as large (0.5-1- mum diameter), collapsed vesicles. The surfaces of flattened, open (i.e., ripped) vesicles often exhibit extended two-dimensional arrays of subunits are arranged into hexagons within each parallelogram unit cell, 12.6x11.1 nm (lattice angle = 109 degrees). The Rockefeller University Press 1982-09-01 /pmc/articles/PMC2112230/ /pubmed/6215413 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
Mannella, CA
Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from neurospora crassa mitochondria
title Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from neurospora crassa mitochondria
title_full Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from neurospora crassa mitochondria
title_fullStr Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from neurospora crassa mitochondria
title_full_unstemmed Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from neurospora crassa mitochondria
title_short Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from neurospora crassa mitochondria
title_sort structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from neurospora crassa mitochondria
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112230/
https://www.ncbi.nlm.nih.gov/pubmed/6215413
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