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Thromb Haemost 1970; 24(01/02): 256-264
DOI: 10.1055/s-0038-1654232
Originalarbeiten – Original Articles – Travaux Originaux
Schattauer GmbH

Factor XIII Assay by an Isotope Method II. Heparin Inhibition of Factor XIII Activation

Alexander Dvilansky
1   Research Fellow in Hematology, New England Medical Center Hospitals, Boston, Massachusetts
,
Anthony F H. Britten   *
2   Director, Blood Coagulation Laboratory, New England Medical Center Hospitals and Assistant Professor of Medicine, Tufts University School of Medicine, Boston, Massachusetts
,
Ariel G Loewy
3   Professor of Biology, Haverford College, Haverford, Pennsylvania
› Author AffiliationsThese studies were supported with funds from the National Institutes of Health General Research Support Grant No. SO 1 FR 05598-04 and National Heart Institute Grant number HE 04385.
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Publication Date:
04 September 2018 (online)

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Summary

A radioisotope method has been used for measuring factor XIII activity. The incorporation of 14C putrescine into casein is used as a model, substituting for the physiologic transamidation fibrin-fibrin bond.

The reaction takes place in two phases, activation of factor XIII by thrombin, and incorporation of 14C putrescine by the active enzyme (transamidase). Heparin inhibits the activation of factor XIII but has no effect upon the active enzyme (transamidase). This heparin effect requires a “co-factor” and does not occur when purified factor XIII is the source of enzyme activity. Protamine sulfate can neutralize the heparin effect if added before the reaction heparin + “co-factor” + thrombin can take place. The heparin inhibition is due to rapid thrombin neutralization, analogous to the heparin anticoagulant effect. Protamine sulfate alone ha s no effect upon either the activation or enzyme phase of factor XIII activity.

* Dr. Anthony F. H. Britten is a Staff Member supported by U. S. Public Health Service Graduate Training Grant no. AM 5210-10 from the National Institutes of Arthritis and Metabolic Diseases.


 

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