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Production of Unsaturated Uronides by Bacterial Hyaluronidases

Nature volume 174, pages 1192–1193 (1954)Cite this article

Abstract

PNEUMOCOCCAL hyaluronidase has been shown to hydrolyse only the glucosaminidic bonds of hyaluronate1. The pneumococcal enzyme and other bacterial hyaluronidases have further been shown to differ from hyaluronidases of animal origin in their thermal lability, and in their capacity to hydrolyse hyaluronate faster and more completely. The main product of exhaustive hydrolysis of hyaluronate by testicular hyaluronidase is a tetrasaccharide2, whereas the end-product of the action of pneumococcal hyaluronidase is a fraction having the reducing values of a disaccharide1.

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References

  1. Rapport, M. M., Linker, A., and Meyer, K., J. Biol. Chem., 192, 283 (1951).

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  2. Weissmann, B., Meyer, K., Sampson, P., and Linker, A., J. Biol. Chem., 208, 417 (1954).

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Authors and Affiliations

  1. Department of Medicine, College of Physicians and Surgeons, Columbia University,

    ALFRED LINKER & KARL MEYER

  2. the Edward Daniels Faulkner Arthritis Clinic of the Presbyterian Hospital, New York

    ALFRED LINKER & KARL MEYER

Authors
  1. ALFRED LINKER
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  2. KARL MEYER
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LINKER, A., MEYER, K. Production of Unsaturated Uronides by Bacterial Hyaluronidases. Nature 174, 1192–1193 (1954). https://doi.org/10.1038/1741192a0

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