An expanding area of interest is the modification of the in vivo clearance of potentially therapeutic proteins. Fate of mutant recombinant albumin molecules in vivo in rabbits. Gene fusion approaches to extending the plasma and whole body half-life of small antithrombotic proteins such as hirudin and barbourin, and the investigation of their antithrombotic properties in vivo.
Intracellular events determine the fate of antithrombin Utah.
Potent antithrombin activity and delayed clearance from the circulation characterize recombinant hirudin genetically fused to albumin. Impact of mutations at P4 on the reaction of antithrombin with thrombin and elastase. Modulation of clearance of recombinant serum albumin by either glycosylation or truncation. A barbourin-albumin fusion protein that is slowly cleared in vivo retains the ability to inhibit platelet aggregation in vitro. Prolonged in vivo anticoagulant activity of a hirudin-albumin fusion protein secreted from Pichia pastoris.