THE ULTRASTRUCTURE OF HUMAN THYROGLOBULIN

Thyroglobulin molecules purified in a single step procedure by gel filtration were studied in the electron microscope using the negative staining technique. The molecule had the shape of a flexible helix with two turns. Its length was about 220 A and the maximal diameter of the coiled part of the mo...

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Detalles Bibliográficos
Autores principales: Bloth, B., Bergquist, R.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1968
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138561/
https://www.ncbi.nlm.nih.gov/pubmed/4971602
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author Bloth, B.
Bergquist, R.
author_facet Bloth, B.
Bergquist, R.
author_sort Bloth, B.
collection PubMed
description Thyroglobulin molecules purified in a single step procedure by gel filtration were studied in the electron microscope using the negative staining technique. The molecule had the shape of a flexible helix with two turns. Its length was about 220 A and the maximal diameter of the coiled part of the molecule was estimated to be 110 A. The pitch varied between 40 and 50 A. Thyroglobulin molecules dried in sodium tungstosilicate on a carbon film as for electron microscopy retained their hemagglutination-inhibiting activity and 19S sedimentation constant when redissolved in physiological buffer.
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spelling pubmed-21385612008-04-17 THE ULTRASTRUCTURE OF HUMAN THYROGLOBULIN Bloth, B. Bergquist, R. J Exp Med Article Thyroglobulin molecules purified in a single step procedure by gel filtration were studied in the electron microscope using the negative staining technique. The molecule had the shape of a flexible helix with two turns. Its length was about 220 A and the maximal diameter of the coiled part of the molecule was estimated to be 110 A. The pitch varied between 40 and 50 A. Thyroglobulin molecules dried in sodium tungstosilicate on a carbon film as for electron microscopy retained their hemagglutination-inhibiting activity and 19S sedimentation constant when redissolved in physiological buffer. The Rockefeller University Press 1968-10-31 /pmc/articles/PMC2138561/ /pubmed/4971602 Text en Copyright © 1968 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
Bloth, B.
Bergquist, R.
THE ULTRASTRUCTURE OF HUMAN THYROGLOBULIN
title THE ULTRASTRUCTURE OF HUMAN THYROGLOBULIN
title_full THE ULTRASTRUCTURE OF HUMAN THYROGLOBULIN
title_fullStr THE ULTRASTRUCTURE OF HUMAN THYROGLOBULIN
title_full_unstemmed THE ULTRASTRUCTURE OF HUMAN THYROGLOBULIN
title_short THE ULTRASTRUCTURE OF HUMAN THYROGLOBULIN
title_sort ultrastructure of human thyroglobulin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138561/
https://www.ncbi.nlm.nih.gov/pubmed/4971602
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