Abstract: Methods for stabilizing lyophilized blood proteins, preferably fibrinogen, comprise forming a stable complex between the blood protein and hydroxypropyl-&agr;-cyclodextrin in an aqueous solution. Hydroxypropyl-&agr;-cyclodextrin is added to the blood protein in an amount sufficient to form a stable complex with the protein. The solution is lyophilized to form a lyophilized protein/hydroxypropyl-&agr;-cyclodextrin complex. The lyophilized protein/hydroxypropyl-&agr;-cyclodextrin complex is then reconsitituted.

Abstract: The present invention relates to a process for purifying Factor IX from an impure protein fraction containing Factor IX. The purification process comprises the steps of adding a solvent and a detergent to an impure protein fraction and incubating the solvent/detergent protein solution to inactivate any viral contaminants. Factor IX is purified from the solvent/detergent protein solution by chromatography on a sulfated polysaccharide resin without first removing the solvent and detergent prior to the purification on the sulfated polysaccharide resin. The Factor IX, purified by the process has a specific activity of at least 85 units/mg.

Abstract: The present invention describes a process for activating Factor II to Factor II.sub.a by incubating Factor II in the presence of Factor V, Factor X.sub.a, phospholipids, and calcium ions. Each of the factors is prepared from a single impure protein fraction which includes Factors II, V and X. The Factor II, V and X purification procedure comprises the steps of DEAE ligand chromatography and precipitation by the addition of barium chloride. Factor V is recovered from the barium chloride supernatant, and Factors II and X are contained in the barium chloride precipitate. The barium chloride precipitate is dissolved in an aqueous solution and is applied to a chromatographic resin coupled with a ligand which binds Factor X and Factor II weakly or not at all. Factor II is recovered from the fraction, which remains unbound or weakly bound to the Factor X binding ligand. Factor X.sub.

Abstract: There is provided, in accordance with practice of this invention, a process for separating Factor IX and/or Factor X from an impure protein fraction containing protein in addition to Factors IX and X. A silica resin coupled with a ligand capable of binding Factor IX and/or Factor X is provided. An aqueous solution of the impure protein fraction is applied to the ligand-coupled silica resin to thereby bind the Factor IX and/or Factor X to the resin. The Factor IX and/or Factor X is then recovered from the resin by elution.

Abstract: A rapid and simple process for purifying human, bovine and porcine procoagulant protein Factor VIII on a large scale using sequential high performance size exclusion chromatography under, first, low salt concentration conditions and, second, under high salt concentration conditions from reconstituted commercial Factor VIII:C (complexed Factor VIII) concentrate. The chromatographic separation is carried out on a high performance size exclusion chromatographic column packed with porous beads having a particle size of from about 13 to about 35 microns, pore diameters of from about 500 to about 2000 Angstroms and a pore volume of from about 1.0 to about 1.8 ml per gram. The first chromatographic separation is carried in a buffered aqueous solution using the buffered aqueous solution as an eluant. The low molecular weight constituents (impurities) are separated from Factor VIII and the high molecular weight constituents (impurities).