Factor XIII Assay by an Isotope Method II. Heparin Inhibition of Factor XIII Activation
| Autor: | Alexander Dvilansky, Anthony F. H. Britten, Ariel G. Loewy |
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| Rok vydání: | 1970 |
| Předmět: | |
| Zdroj: | Thrombosis and Haemostasis. 24:256-264 |
| ISSN: | 2567-689X 0340-6245 |
| DOI: | 10.1055/s-0038-1654232 |
| Popis: | SummaryA 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. |
| Databáze: | OpenAIRE |
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