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

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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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