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CHARACTERIZATION OF THE EXTERNAL PROTEINS OF HAMSTER FIBROBLASTS

The results of metabolic labeling studies and enzymatic treatments followed by analysis on polyacrylamide gels show that the external proteins of hamster fibroblast cell lines, which have been identified by lactoperoxidase-catalyzed iodination, do not contain sulphated mucopolysaccharides or hyaluro...

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Detalles Bibliográficos
Autores principales: Hynes, Richard O., Humphryes, Kenneth C.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1974
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2109387/
https://www.ncbi.nlm.nih.gov/pubmed/4372240
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author Hynes, Richard O.
Humphryes, Kenneth C.
author_facet Hynes, Richard O.
Humphryes, Kenneth C.
author_sort Hynes, Richard O.
collection PubMed
description The results of metabolic labeling studies and enzymatic treatments followed by analysis on polyacrylamide gels show that the external proteins of hamster fibroblast cell lines, which have been identified by lactoperoxidase-catalyzed iodination, do not contain sulphated mucopolysaccharides or hyaluronic acid and are probably unrelated to collagen. Several of the iodinated species comigrate with carbohydrate-containing molecules. In particular, the major iodine-labeled polypeptide of normal fibroblasts appears to be a glycoprotein. This glycoprotein is absent or much reduced in virus-transformed cells, as detected both by iodination and by metabolic labeling. We conclude that the major iodinated polypeptide is not detected on transformed cells because it is absent rather than because it is masked. Approximate molecular weights of the external proteins are also reported.
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spelling pubmed-21093872008-05-01 CHARACTERIZATION OF THE EXTERNAL PROTEINS OF HAMSTER FIBROBLASTS Hynes, Richard O. Humphryes, Kenneth C. J Cell Biol Article The results of metabolic labeling studies and enzymatic treatments followed by analysis on polyacrylamide gels show that the external proteins of hamster fibroblast cell lines, which have been identified by lactoperoxidase-catalyzed iodination, do not contain sulphated mucopolysaccharides or hyaluronic acid and are probably unrelated to collagen. Several of the iodinated species comigrate with carbohydrate-containing molecules. In particular, the major iodine-labeled polypeptide of normal fibroblasts appears to be a glycoprotein. This glycoprotein is absent or much reduced in virus-transformed cells, as detected both by iodination and by metabolic labeling. We conclude that the major iodinated polypeptide is not detected on transformed cells because it is absent rather than because it is masked. Approximate molecular weights of the external proteins are also reported. The Rockefeller University Press 1974-08-01 /pmc/articles/PMC2109387/ /pubmed/4372240 Text en Copyright © 1974 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
Hynes, Richard O.
Humphryes, Kenneth C.
CHARACTERIZATION OF THE EXTERNAL PROTEINS OF HAMSTER FIBROBLASTS
title CHARACTERIZATION OF THE EXTERNAL PROTEINS OF HAMSTER FIBROBLASTS
title_full CHARACTERIZATION OF THE EXTERNAL PROTEINS OF HAMSTER FIBROBLASTS
title_fullStr CHARACTERIZATION OF THE EXTERNAL PROTEINS OF HAMSTER FIBROBLASTS
title_full_unstemmed CHARACTERIZATION OF THE EXTERNAL PROTEINS OF HAMSTER FIBROBLASTS
title_short CHARACTERIZATION OF THE EXTERNAL PROTEINS OF HAMSTER FIBROBLASTS
title_sort characterization of the external proteins of hamster fibroblasts
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2109387/
https://www.ncbi.nlm.nih.gov/pubmed/4372240
work_keys_str_mv AT hynesrichardo characterizationoftheexternalproteinsofhamsterfibroblasts
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