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Hemophilia A Therapy

Addition of a disulfide bond to factor VIIIa prolongs its life in blood

Published in Hematology Week, November 10th, 2003

Addition of a disulfide bond to factor VIIIa prolongs its life in blood, stabilizing the protein.

According to a study from the United States, "The blood coagulation disorder, hemophilia A, is caused by deficiency of coagulation factor FVIII. Hemophilia A is now treated by infusions of pure FVIII, but the activity of FVIII is limited, because it is unstable following activation by thrombin. This instability of activated FVIII is the result of dissociation of the A2 subunit.

"To obtain increased stability in FVIIIa, a disulfide bond between the A2 domain and the A3 domain, preventing A2 subunit dissociation, has been engineered. Structural analysis of...

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