Thromb Haemost 1969; 22(01): 045-067
DOI: 10.1055/s-0038-1651328
Originalarbeiten-Original Articles-Travaux Originaux
Schattauer GmbH

The Human Prothrombin-Activating Enzyme[*]

K Deggeller
1   Central Laboratory of the Netherlands Red Cross Blood Transfusion Service (Director: Prof. Dr. J. J. van Loghem), Amsterdam, The Netherlands
,
J Vreeken
1   Central Laboratory of the Netherlands Red Cross Blood Transfusion Service (Director: Prof. Dr. J. J. van Loghem), Amsterdam, The Netherlands
› Author Affiliations
Further Information

Publication History

Publication Date:
10 June 2018 (online)

Summary

The formation and action of human prothrombin-activating enzyme is described. The study of the formation of the enzyme leads to the following conclusions :

1. The enzyme is formed from factor V, factor X and phospholipid in the presence of calcium. If one of the reagents is omitted no activity develops.

2. Factor V and factor X need activation by thrombin and for instance Russell Viper Venom, respectively.

3. A linear relationship exists between the inverse of factor Va concentration and the inverse of enzyme concentration.

4. A linear relationship exists between the inverse of factor Xa concentration and the inverse of enzyme concentration.

5. A linear relationship exists between the inverse of phospholipid concentration and the inverse of enzyme concentration at small phospholipid concentration.

6. A linear relationship exists between the phospholipid concentration and the inverse of enzyme concentration at high phospholipid concentration.

The study of the action of the enzyme leads to the conclusion that human prothrombin is substrate and an inhibitor if present in excess.

The observed phenomena are best explained by the hypothesis that factor Va and factor Xa adsorb onto the phospholipid surface. When both factors are adsorbed close together they are active as an enzyme. This activity depends on two active centers, probably one derived from factor Va and one from factor Xa.

* The investigations were supported by the Netherlands Foundation for Chemical Research (SON) with financial aid from the Netherlands Organization for the Advancement of Pure Research (ZWO).


 
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