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Thromb Haemost 1975; 33(03): 553-563
DOI: 10.1055/s-0038-1647849
Original Article
Schattauer GmbH

The Activation of Human Factor IX

B Østerud
1   Institute of Medical Biology, University of Tromsø and Department of Pharmacology, Institute of Pharmacy, University of Oslo, Norway
,
K Laake
1   Institute of Medical Biology, University of Tromsø and Department of Pharmacology, Institute of Pharmacy, University of Oslo, Norway
,
H Prydz
1   Institute of Medical Biology, University of Tromsø and Department of Pharmacology, Institute of Pharmacy, University of Oslo, Norway
› Author Affiliations
Further Information

Publication History

Received 03 September 1974

Accepted 29 November 1974

Publication Date:
02 July 2018 (online)

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Summary

The activation of factor IX purified from human plasma has been studied. Factor XIa and kallikrein separately activated factor IX to factor IXa. In both cases factor IX a had an apparent molecular weight of about 42–45000 in sodium dodecyl sul-phate-polyacrylamide disc gel electrophoresis compared with a molecular weight of about 70000 for the native factor IX. The activation by XIa required Ca2+-ions whereas Ca2+-ions did not influence the activation by kallikrein. A mixture of tissue thromboplastin and factor VII or RusselPs-viper venom alone did not activate factor IX. Trypsin activated and plasmin inactivated factor IX.

 

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