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Electron Microscopy of Chondromucoprotein and the Products of its Digestion with Hyaluronidase and Papain

Nature volume 214, pages 194–195 (1967)Cite this article

Abstract

WHEN chondroitin sulphuric acid is extracted from cartilage in dilute salt solutions, it is always bound to protein1–3. The complex chondromucoprotein has a molecular weight of more than one million, whereas the polysaccharide portion chondroitin sulphuric acid (CSA) has a molecular weight of about 50,000 (refs. 3 and 4). The presently conceived model is that in which the protein forms a core to which chondroitin sulphuric acid is covalently bound at many points, by glycosidic linkage through the hydroxyl group on serine4,5.

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Authors and Affiliations

  1. Department of Pathology, Stanford School of Medicine, Palo Alto, California

    A. M. SAUNDERS & L. SILVERMAN

Authors
  1. A. M. SAUNDERS
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  2. L. SILVERMAN
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SAUNDERS, A., SILVERMAN, L. Electron Microscopy of Chondromucoprotein and the Products of its Digestion with Hyaluronidase and Papain. Nature 214, 194–195 (1967). https://doi.org/10.1038/214194a0

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