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THE MOLECULAR WEIGHT AND ISOELECTRIC POINT OF THYROGLOBULIN
1. The sedimentation constant of hog thyroglobulin is 19.2ċ10(–13). That of human thyroglobulin is essentially the same. 2. The specific volume of hog thyroglobulin is 0.72. 3. The isoelectric point of native hog thyroglobulin is at pH 4.58, that of denatured thyroglobulin at pH 5.0. 4. The molecula...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1935
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141410/ https://www.ncbi.nlm.nih.gov/pubmed/19872918 |
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author | Heidelberger, Michael Pedersen, Kai O. |
author_facet | Heidelberger, Michael Pedersen, Kai O. |
author_sort | Heidelberger, Michael |
collection | PubMed |
description | 1. The sedimentation constant of hog thyroglobulin is 19.2ċ10(–13). That of human thyroglobulin is essentially the same. 2. The specific volume of hog thyroglobulin is 0.72. 3. The isoelectric point of native hog thyroglobulin is at pH 4.58, that of denatured thyroglobulin at pH 5.0. 4. The molecular weight of hog thyroglobulin is, in round numbers, 700,000, as calculated from the sedimentation and diffusion constants, or 650,000, as calculated from the sedimentation equilibrium data. 5. The thyroglobulin molecule deviates markedly from the spherical. |
format | Text |
id | pubmed-2141410 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1935 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21414102008-04-23 THE MOLECULAR WEIGHT AND ISOELECTRIC POINT OF THYROGLOBULIN Heidelberger, Michael Pedersen, Kai O. J Gen Physiol Article 1. The sedimentation constant of hog thyroglobulin is 19.2ċ10(–13). That of human thyroglobulin is essentially the same. 2. The specific volume of hog thyroglobulin is 0.72. 3. The isoelectric point of native hog thyroglobulin is at pH 4.58, that of denatured thyroglobulin at pH 5.0. 4. The molecular weight of hog thyroglobulin is, in round numbers, 700,000, as calculated from the sedimentation and diffusion constants, or 650,000, as calculated from the sedimentation equilibrium data. 5. The thyroglobulin molecule deviates markedly from the spherical. The Rockefeller University Press 1935-09-20 /pmc/articles/PMC2141410/ /pubmed/19872918 Text en Copyright © Copyright, 1935, by The Rockefeller Institute for Medical Research 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 Heidelberger, Michael Pedersen, Kai O. THE MOLECULAR WEIGHT AND ISOELECTRIC POINT OF THYROGLOBULIN |
title | THE MOLECULAR WEIGHT AND ISOELECTRIC POINT OF THYROGLOBULIN |
title_full | THE MOLECULAR WEIGHT AND ISOELECTRIC POINT OF THYROGLOBULIN |
title_fullStr | THE MOLECULAR WEIGHT AND ISOELECTRIC POINT OF THYROGLOBULIN |
title_full_unstemmed | THE MOLECULAR WEIGHT AND ISOELECTRIC POINT OF THYROGLOBULIN |
title_short | THE MOLECULAR WEIGHT AND ISOELECTRIC POINT OF THYROGLOBULIN |
title_sort | molecular weight and isoelectric point of thyroglobulin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141410/ https://www.ncbi.nlm.nih.gov/pubmed/19872918 |
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