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High density of transmembrane glycoproteins on the flagellar surface of boar sperm cells
Membrane halves of boar sperm flagella were produced by freeze-fracture and labeled in situ with concanavalin A and wheat germ agglutinin; the lectins were visualized with protein-gold complexes. Concanavalin A and wheat germ agglutinin binding sites partition with both protoplasmic and exoplasmic h...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1984
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113257/ https://www.ncbi.nlm.nih.gov/pubmed/6746741 |
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collection | PubMed |
description | Membrane halves of boar sperm flagella were produced by freeze-fracture and labeled in situ with concanavalin A and wheat germ agglutinin; the lectins were visualized with protein-gold complexes. Concanavalin A and wheat germ agglutinin binding sites partition with both protoplasmic and exoplasmic halves of the membrane. A high density of lectin marking was found on protoplasmic membrane halves; we conclude that the label corresponds to transmembrane glycoproteins that, on freeze-fracture, are dragged across the outer (exoplasmic) half of the phospholipid bilayer. Our demonstration of numerous transmembrane proteins in sperm flagella offers the structural setting for previous models on flagellar surface motility that postulate accessibility of motile membrane components to the submembranous cytoskeleton. |
format | Text |
id | pubmed-2113257 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1984 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21132572008-05-01 High density of transmembrane glycoproteins on the flagellar surface of boar sperm cells J Cell Biol Articles Membrane halves of boar sperm flagella were produced by freeze-fracture and labeled in situ with concanavalin A and wheat germ agglutinin; the lectins were visualized with protein-gold complexes. Concanavalin A and wheat germ agglutinin binding sites partition with both protoplasmic and exoplasmic halves of the membrane. A high density of lectin marking was found on protoplasmic membrane halves; we conclude that the label corresponds to transmembrane glycoproteins that, on freeze-fracture, are dragged across the outer (exoplasmic) half of the phospholipid bilayer. Our demonstration of numerous transmembrane proteins in sperm flagella offers the structural setting for previous models on flagellar surface motility that postulate accessibility of motile membrane components to the submembranous cytoskeleton. The Rockefeller University Press 1984-08-01 /pmc/articles/PMC2113257/ /pubmed/6746741 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 High density of transmembrane glycoproteins on the flagellar surface of boar sperm cells |
title | High density of transmembrane glycoproteins on the flagellar surface of boar sperm cells |
title_full | High density of transmembrane glycoproteins on the flagellar surface of boar sperm cells |
title_fullStr | High density of transmembrane glycoproteins on the flagellar surface of boar sperm cells |
title_full_unstemmed | High density of transmembrane glycoproteins on the flagellar surface of boar sperm cells |
title_short | High density of transmembrane glycoproteins on the flagellar surface of boar sperm cells |
title_sort | high density of transmembrane glycoproteins on the flagellar surface of boar sperm cells |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113257/ https://www.ncbi.nlm.nih.gov/pubmed/6746741 |