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THE FINE STRUCTURE OF BOVINE NASAL CARTILAGE : Extraction as a Technique to Study Proteoglycans and Collagen in Cartilage Matrix
Bovine nasal cartilage was studied by electron microscopy before and after extraction with 4 M guanidinium chloride or 1.9 M CaCl(2). These solvents removed matrix granules, basophilia, and 85% of the proteoglycan complex, measured as hexuronate. Simultaneously, many collagen fibrils were disaggrega...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1971
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2108507/ https://www.ncbi.nlm.nih.gov/pubmed/4103953 |
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author | Anderson, H. Clarke Sajdera, Stanley W. |
author_facet | Anderson, H. Clarke Sajdera, Stanley W. |
author_sort | Anderson, H. Clarke |
collection | PubMed |
description | Bovine nasal cartilage was studied by electron microscopy before and after extraction with 4 M guanidinium chloride or 1.9 M CaCl(2). These solvents removed matrix granules, basophilia, and 85% of the proteoglycan complex, measured as hexuronate. Simultaneously, many collagen fibrils were disaggregated into component microfibrils (approximately 40 A thick). In contrast to the above solvents, exhaustive extraction with 0.5 M guanidinium chloride removed 20% of the proteoglycan complex, and matrix granules were reduced in size but not in number. Extraction with 4 M CaCl(2) removed only 10% of the proteoglycan complex, did not remove matrix granules, and caused the normal banding pattern of collagen to disappear. The banding was restored by further treatment with trypsin. Trypsin, before or after 4 M CaCl(2), removed matrix granules and 90% of the proteoglycan complex. We conclude that matrix granules are an electron microscopic representation of the proteoglycan complex, and consist of more than one proteoglycan macromolecule. It would appear that 4 M guanidinium chloride and 1.9 M CaCl(2), in addition to removing most of the proteoglycan complex, also disaggregate some of the collagen fibrils into their component microfibrils. |
format | Text |
id | pubmed-2108507 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1971 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21085072008-05-01 THE FINE STRUCTURE OF BOVINE NASAL CARTILAGE : Extraction as a Technique to Study Proteoglycans and Collagen in Cartilage Matrix Anderson, H. Clarke Sajdera, Stanley W. J Cell Biol Article Bovine nasal cartilage was studied by electron microscopy before and after extraction with 4 M guanidinium chloride or 1.9 M CaCl(2). These solvents removed matrix granules, basophilia, and 85% of the proteoglycan complex, measured as hexuronate. Simultaneously, many collagen fibrils were disaggregated into component microfibrils (approximately 40 A thick). In contrast to the above solvents, exhaustive extraction with 0.5 M guanidinium chloride removed 20% of the proteoglycan complex, and matrix granules were reduced in size but not in number. Extraction with 4 M CaCl(2) removed only 10% of the proteoglycan complex, did not remove matrix granules, and caused the normal banding pattern of collagen to disappear. The banding was restored by further treatment with trypsin. Trypsin, before or after 4 M CaCl(2), removed matrix granules and 90% of the proteoglycan complex. We conclude that matrix granules are an electron microscopic representation of the proteoglycan complex, and consist of more than one proteoglycan macromolecule. It would appear that 4 M guanidinium chloride and 1.9 M CaCl(2), in addition to removing most of the proteoglycan complex, also disaggregate some of the collagen fibrils into their component microfibrils. The Rockefeller University Press 1971-06-01 /pmc/articles/PMC2108507/ /pubmed/4103953 Text en Copyright © 1971 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 Anderson, H. Clarke Sajdera, Stanley W. THE FINE STRUCTURE OF BOVINE NASAL CARTILAGE : Extraction as a Technique to Study Proteoglycans and Collagen in Cartilage Matrix |
title | THE FINE STRUCTURE OF BOVINE NASAL CARTILAGE : Extraction as a Technique to Study Proteoglycans and Collagen in Cartilage Matrix |
title_full | THE FINE STRUCTURE OF BOVINE NASAL CARTILAGE : Extraction as a Technique to Study Proteoglycans and Collagen in Cartilage Matrix |
title_fullStr | THE FINE STRUCTURE OF BOVINE NASAL CARTILAGE : Extraction as a Technique to Study Proteoglycans and Collagen in Cartilage Matrix |
title_full_unstemmed | THE FINE STRUCTURE OF BOVINE NASAL CARTILAGE : Extraction as a Technique to Study Proteoglycans and Collagen in Cartilage Matrix |
title_short | THE FINE STRUCTURE OF BOVINE NASAL CARTILAGE : Extraction as a Technique to Study Proteoglycans and Collagen in Cartilage Matrix |
title_sort | fine structure of bovine nasal cartilage : extraction as a technique to study proteoglycans and collagen in cartilage matrix |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2108507/ https://www.ncbi.nlm.nih.gov/pubmed/4103953 |
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