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The Journal of Cell Biology, Vol 49, 650-663, Copyright © 1971 by Rockefeller University Press

ARTICLE

THE FINE STRUCTURE OF BOVINE NASAL CARTILAGE : Extraction as a Technique to Study Proteoglycans and Collagen in Cartilage Matrix



H. Clarke Anderson 1 and Stanley W. Sajdera 1

1 From the Department of Pathology and the Program in Physical and Organic Chemistry, State University of New York, Downstate Medical Center, Brooklyn, New York 11203, and The Rockefeller University, New York 10021

Bovine nasal cartilage was studied by electron microscopy before and after extraction with 4 M guanidinium chloride or 1.9 M CaCl2. 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 CaCl2 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 CaCl2, 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 CaCl2, in addition to removing most of the proteoglycan complex, also disaggregate some of the collagen fibrils into their component microfibrils.

 Submitted on August 18, 1970
Revised on December 30, 1970


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