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Broad Specificity Inhibitors from Sea Anemones

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Proteinase Inhibitors

Part of the book series: Bayer-Symposium ((BAYER-SYMP,volume 5))

Abstract

40 years after the discovery of a low molecular weight kallikrein inhibitor in bovine organs by Frey, Kraut, and Werle [1], Béress et al found similar inhibitors in sea anemones [2, 3]. These inhibitors show the same inhibition specifity [3, 4] as the trypsin-kallikrein inhibitor (BPTI) which occurs only in Bovinae and Caprinae. The biological function of inhibitors in sea anemones is unknown, but it is interesting that the highest concentration appears in the tentacles [5].

Supported by Sonderforschungsbereich 51, München and Deutsche Forschungsgemeinschaft (L.B.).

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References

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© 1974 Springer-Verlag

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Wunderer, G., Kummer, K., Fritz, H., Béress, L., Machleidt, W. (1974). Broad Specificity Inhibitors from Sea Anemones. In: Fritz, H., Tschesche, H., Greene, L.J., Truscheit, E. (eds) Proteinase Inhibitors. Bayer-Symposium, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-87966-1_32

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  • DOI: https://doi.org/10.1007/978-3-642-87966-1_32

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-87968-5

  • Online ISBN: 978-3-642-87966-1

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