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Multiple Specificity of Thrombin for Synthetic Substrates

Nature volume 213, pages 405–406 (1967)Cite this article

Abstract

THE original work on the activity of thrombin on synthetic substrates1 indicated that its hydrolytic action was confined to the arginine esters and amides, but more recent investigations2 have shown that the specificity of thrombin is very similar to that of trypsin, which hydrolyses both arginine and lysine esters. We have recently reported that thrombin also hydrolyses phenylalanine and tyrosine ester substrates (unpublished results), and we have therefore investigated the enzyme activity of thrombin towards a variety of amino-acid esters, to define more precisely the specificity of the enzyme.

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Authors and Affiliations

  1. Coagulation Research Laboratory, Division of Surgery, Presbyterian–St. Luke's Hospital, Chicago, Illinois

    EDMOND R. COLE, J. L. KOPPEL & JOHN H. OLWIN

Authors
  1. EDMOND R. COLE
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  2. J. L. KOPPEL
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  3. JOHN H. OLWIN
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COLE, E., KOPPEL, J. & OLWIN, J. Multiple Specificity of Thrombin for Synthetic Substrates. Nature 213, 405–406 (1967). https://doi.org/10.1038/213405a0

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