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

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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