Letter | Published:

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

Naturevolume 214pages194195 (1967) | Download Citation

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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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References

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    Partridge, S. M., Davis, H. F., and Adair, G. S., ibid., 79, 15 (1961).

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    Gregory, J., and Roden, L., Biochem. Biophys. Res. Commun., 5, 430 (1961).

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Affiliations

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

    • A. M. SAUNDERS
    •  & L. SILVERMAN

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https://doi.org/10.1038/214194a0

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