Abstract: The invention provides processes for producing preparations (e.g., plasma preparations or fibrinogen (Fg)-depleted preparations) containing one or more proteins (e.g., plasma proteins). Processes of the invention can be used to obtain enriched preparations of one or more proteins (e.g., Fg, immunoglobulin (Ig; e.g., IgG), alpha-1 proteinase inhibitor (A1 PI), albumin, plasminogen, prothrombin complex, and/or other plasma proteins). Multiple enriched preparations can be obtained from a single sample (e.g., a whole blood or plasma sample) using the processes of the invention.

Abstract: Peptides that have domains that bind to recombinant factor VIII (rFVIII) are disclosed. A method of rFVIII binding assay using the peptides deduced from a combinatorial library in a filtration plate process is described. A method of using peptides having these available binding domains in an affinity chromatography process to purify factor VIII is also taught.

Abstract: The invention is a method of purifying Factor VIII comprising the steps of contacting a solution containing Factor VIII with a Factor VIII-binding substrate under conditions sufficient to bind Factor VIII to the substrate, wherein the Factor VIII-binding substrate comprises one or more peptides bound to the substrate, wherein the peptides are selected from the group consisting of SEQ ID NO:1, SEQ ID NO:2, and SEQ ID NO:3, and then eluting the bound Factor VIII.

Abstract: Peptides which bind Factor VIII are disclosed. The peptides have available Factor VIII binding domains having a Trp-His-Tyr-Tyr-His-Gly, His-Ile-Gln-His-Tyr-His, or His-Gln-Tyr-Gly-Tyr-His sequence. Peptides having at least one of these Factor VIII binding domains are immobilized upon a chromatographic substrate in a preferred embodiment of the invention. This preferred embodiment is useful in a chromatography process to purify human Factor VIII.

Abstract: Ligands that interact with a target can be more easily identified if false positive interactions (either specific or non-specific) from the detecting system are differentiated from the target-specific interaction. An improved method of identifying peptides which bind with a target protein is presented. The steps are: binding a random library of peptides to a support material, allowing detection reagents to contact the peptides and the support material then identifying these interactions, then allowing the target protein to selectively bind to the peptides, allowing detection reagents to contact the bound target protein, and characterizing the peptide bound to the identified support material. Interaction of a ligand or the support material with the detection reagents will cause a distinct color change which distinguishes those ligands which selectively bind to target protein. The characterized peptide can then be used in affinity purification of the target protein.

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 Trp-Gln-Glu-His-Tyr-Asn, Trp-Gln-Glu-Thr-TyrGln,or Tyr-Glu-Asn-Tyr-Gly-Tyr sequence. Peptides containing at least one of these fibrinogen binding domains are immobilized upon a chromatographic substrate in a preferred embodiment of the invention. This preferred embodiment is useful in an affinity chromatography process to purify fibrinogen.

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.