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Thromb Haemost 1958; 02(03/04): 205-217
DOI: 10.1055/s-0038-1656273
Originalarbeiten — Original Articles — Travaux Originaux
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The Mode of Action of Thrombin

K Laki
1   National Institute of Arthritis and Metabolic Diseases and National Institute of Dental Research ; National Institutes of Health; Public Health Service; U.S. Department of Health, Education, and Welfare, Bethesda, Maryland
,
Jules A. Gladner
1   National Institute of Arthritis and Metabolic Diseases and National Institute of Dental Research ; National Institutes of Health; Public Health Service; U.S. Department of Health, Education, and Welfare, Bethesda, Maryland
,
J. E Folk   *
1   National Institute of Arthritis and Metabolic Diseases and National Institute of Dental Research ; National Institutes of Health; Public Health Service; U.S. Department of Health, Education, and Welfare, Bethesda, Maryland
,
D. R Kominz
1   National Institute of Arthritis and Metabolic Diseases and National Institute of Dental Research ; National Institutes of Health; Public Health Service; U.S. Department of Health, Education, and Welfare, Bethesda, Maryland
› Author Affiliations
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Publication History

Publication Date:
07 June 2018 (online)

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Summary

The peptides liberated from fibrinogen by the action of thrombin have been isolated on modified cellulose adsorbents. These peptides have been characterized by sedimentation-diffusion measurements by quantitative amino acid analysis, and by C-terminal analysis. Both peptides were found to contain arginine as C-terminal amino acid. Thrombin thus splits specific arginyl-glycine bonds in the fibrinogen molecule. The specificity of thrombin is discussed in view of the finding that the active center of thrombin is similar to that of trypsin and chymotrypsin.

* National Institute of Dental Research.


 

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