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

Alexander Dvilansky; Anthony F H. Britten; Ariel G Loewy

doi:10.1055/s-0038-1654232

Thrombosis and Haemostasis, Table of Contents

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

¹Research Fellow in Hematology, New England Medical Center Hospitals, Boston, Massachusetts

,

Anthony F H. Britten^*

²Director, Blood Coagulation Laboratory, New England Medical Center Hospitals and Assistant Professor of Medicine, Tufts University School of Medicine, Boston, Massachusetts

,

Ariel G Loewy

³Professor of Biology, Haverford College, Haverford, Pennsylvania

› Author Affiliations

Abstract

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.

Full Text

References

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