Proteolytic inactivation of human factor VIII procoagulant protein by activated human protein C and its analogy with factor V
| Autor: | CA Fulcher, JE Gardiner, JH Griffin, TS Zimmerman |
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| Rok vydání: | 1984 |
| Předmět: | |
| Zdroj: | Blood. 63:486-489 |
| ISSN: | 1528-0020 0006-4971 |
| DOI: | 10.1182/blood.v63.2.486.486 |
| Popis: | Purified human factor VIII procoagulant protein (VIII:C) was treated with purified human activated protein C (APC) and the loss of VIII:C activity correlated with proteolysis of the VIII:C polypeptides. APC proteolyzed all VIII:C polypeptides with mol wt = 92,000 or greater, but not the doublet at mol wt = 79–80,000. These results and our previous thrombin activation studies of purified VIII:C, are analogous with similar studies of factor V and form the basis for the following hypothesis: activated VIII:C consists of heavy and light chain polypeptides [mol wt = 92,000 and mol wt = 79–80,000 (or 71–72,000), respectively] which are similar in Mr to the heavy and light chains of activated factor V. Thrombin activates VIII:C and V by generating these polypeptide chains from larger precursors and APC inactivates both molecules by cleavage at a site located in the heavy chain region of activated VIII:C and V. |
| Databáze: | OpenAIRE |
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