Abstract: Disclosed herein are methods and composition producing a viral vaccine with reduced particle size, particularly for use in the production of influenza virus vaccines.

Abstract: Purification of ?-1 proteinase inhibitor (?-1 PI) from solutions comprising ?-1 PI is accomplished using hydrophobic interaction chromatography (HIC). In some embodiments, purification of ?-1 PI is accomplished by precipitation of contaminating proteins from a starting solution comprising ?-1 PI, such as human plasma, followed by anion exchange resin chromatography prior to HIC. Further purification may be accomplished by an optional cation exchange chromatography subsequent to anion exchange chromatography but prior to HIC. Some embodiments of the invention also include virus removal and/or inactivation by methods such as nano filtration and such as contact with a non-ionic detergent. The methods of the present invention result in greater yield, purity, and pathogenic clearance of plasma fractions than known methods.

Abstract: Disclosed is both a process for producing a reversibly inactive acidified plasmin by activating plasminogen and a process for producing a purified plasminogen. The produced plasmin is isolated and stored with a low pH-buffering capacity agent to provide a substantially stable formulation. The purified plasminogen is typically purified from a fraction obtained in the separation of immunoglobulin from Fraction II+III chromatographic process and eluted at a low pH. The reversibly inactive acidified plasmin may be used in the administration of a thrombolytic therapy.

Abstract: Disclosed is both a process for producing a reversibly inactive acidified plasmin by activating plasminogen and a process for producing a purified plasminogen. The produced plasmin is isolated and stored with a low pH-buffering capacity agent to provide a substantially stable formulation. The purified plasminogen is typically purified from a fraction obtained in the separation of immunoglobulin from Fraction II+III chromatographic process and eluted at a low pH. The reversibly inactive acidified plasmin may be used in the administration of a thrombolytic therapy.

Abstract: Disclosed is both a process for producing a reversibly inactive acidified plasmin by activating plasminogen and a process for producing a purified plasminogen. The produced plasmin is isolated and stored with a low pH-buffering capacity agent to provide a substantially stable formulation. The purified plasminogen is typically purified from a fraction obtained in the separation of immunoglobulin from Fraction II+III chromatographic process and eluded at a low pH. The reversibly inactive acidified plasmin may be used in the administration of a thrombolytic therapy.

Abstract: A method and device for activating and applying a solution of fibrinogen to form fibrin glue at a desired site. The method includes contacting the solution of fibrinogen with immobilized thrombin under conditions that result in a solution of polymerizable fibrin and delivering the activated solution to the desired site. The device includes a housing having a compartment for a solution of fibrinogen, a container for immobilized thrombin, a structure following the solution of fibrinogen to be brought into contact with the immobilized thrombin under conditions which permit the activation of the fibrinogen to polymerizable fibrin, and a structure allowing for delivery of the activated solution to the desired site.

Abstract: A method and device for activating and applying a solution of fibrinogen to a desired site. The method includes contacting the solution of fibrinogen with immobilized thrombin resulting in an activated solution of polymerizable fibrin, and delivering the activated solution to the desired site. The device includes a housing having a compartment for a solution of fibrinogen, immobilized thrombin, a structure for bringing the solution of fibrinogen in contact with the immobilized thrombin under conditions which permit the activation of the fibrinogen resulting in polymerizable fibrin, and a structure for delivery of the activated solution to the desired site.

Abstract: Peptide ligands which bind to thrombin and prothrombin are disclosed. The sequences of these peptides are Gln-Leu-Trp-Gly-Ser-His, Arg-Gln-Leu-Trp-Gly-Ser-His, His-Gln-Leu-Trp-Gly-Ser-His, and Tyr-Phe-Pro-Gly-Pro-Tyr-Leu. The preferred peptides have the sequence Gln-Leu-Trp-Gly-Ser-His or Tyr-Phe-Pro-Gly-Pro-Tyr-Leu. A method of using these peptides in an affinity chromatography process to purify thrombin is described.

Abstract: Peptides which bind to fibrinogen are disclosed. These peptides have available fibrinogen binding domains having a Phe-Leu-Leu-Val or Leu-Leu-Val-Pro sequence. The preferred peptide is a 6-mer having the sequence Phe-Leu-Leu-Val-Pro-Leu (SEQ ID NO:1). A method of using these peptides in an affinity chromatography process to purify fibrinogen is described.

Abstract: Peptide ligands which bind to von Willebrand Factor (vWF) are disclosed. These peptides are selected from the group consisting of RLHSFY, RLKSFY, RLNSFY, RLQSFY, RFRSFY, RIRSFY, RVRSFY, RYRSFY, RLRSFY, HLRSFY, and KLRSFY. The preferred peptide ligand has the sequence RVRSFY. A method of using the disclosed peptides to purify vWF comprises binding the peptides to a support, then passing a solution containing vWF over the supports under condition such that the vWF will selectively bind to the peptides, and then eluting the vWF.