Abstract: A process for reduction and/or removal of FXI and FXIa from a source solution containing said coagulation factors and as main components immunoglobulins comprising the following steps: a) contacting the FXI and/or FXIa containing solution with an affinity chromatographic gel wherein heparin or heparan is linked to the matrix material; b) allowing adsorption of FXI and/or FXIa and c) separation of the liquid deprived of FXI and/or FXIa from the adsorption media.

Abstract: A process of purifying a Growth Factor Protein in a purification sequence employing chromatography characterized in that at least one chromatography is performed using a multimodal resin the Growth Factor Protein binds to the multimodal resin at a pH between 4 to 6.2, and the Growth Factor Protein is eluting at a pH>6.3, and the elution of Growth Factor Protein is improved by addition of arginine and/or NaCl to the eluting buffer. The multimodal resin step is followed by a yeast derived affinity ligand resin step, which results of a purity of the product>90%.

Abstract: A process of manufacturing a prion-free Vitamin K dependent Protein in a purification sequence employing chromatography characterized in that at least one chromatography step is performed using a multimodal resin providing a fraction containing Vitamin K dependent Protein in an aqueous solution; contacting the fraction containing the Vitamin K dependent Protein with a multimodal resin at a pH between 6-9; optionally washing the multimodal resin having the Vitamin K dependent Protein adsorbed with an aqueous washing buffer to wash away contaminants and retain the Vitamin K dependent Protein, before the Vitamin K dependent Protein is eluted; the Vitamin K dependent Protein is eluting from the multimodal resin at a pH between 6 to 9 in a buffer comprising arginine; and optionally collecting Vitamin K dependent Protein containing fractions in purified or enriched form.

Abstract: A process of purifying or enriching coagulation FVIII employing chromatography comprising the steps of providing a fraction containing FVIII in an aqueous solution having a high ionic strength; contacting the fraction containing FVIII with a multimodal resin; optionally washing the multimodal resin having FVIII adsorbed with an aqueous washing buffer; eluting FVIII containing fractions by an aqueous elution buffer comprising at least one amino acid which is positively charged at pH 6 to 8; and optionally collecting FVIII containing fractions in purified or enriched form.

Abstract: A process of purifying or enriching coagulation FVIII employing chromatography comprising the steps of providing a fraction containing FVIII in an aqueous solution having a high ionic strength; contacting the fraction containing FVIII with a multimodal resin; optionally washing the multimodal resin having FVIII adsorbed with an aqueous washing buffer; eluting FVIII containing fractions by an aqueous elution buffer comprising at least one amino acid which is positively charged at pH 6 to 8; and optionally collecting FVIII containing fractions in purified or enriched form.

Abstract: A process for manufacturing of a composition containing a purified factor for supporting wound healing selected from the group consisting of Hepatocyte Growth Factor (HGF) platelet derived growth factor (PDGF), Epidermal growth factor (EGF), transforming growth factor alfa (TGF-?), Transforming growth factor beta (TGF-?), insulin like growth factor (IGF-1) and Fibroblast growth factor (FGF) from sources, such as blood, containing the factor for supporting wound healing, wherein the manufacturing process comprises purification steps which are performed in the presence of antithrombin III (AT-III).

Abstract: A process for isolation and purification of a target protein by chromatography wherein the chromatography removes or depletes prions (PrPSC), comprising the steps of contacting a potentially PrPSC contaminated sample comprising a target protein with a multimodal chromatographic material; setting buffer conditions so that the target protein is bound to the multimodal chromatographic material and whereas PrPSC is not binding to the multimodal chromatographic material; followed by elution of the target protein. a process for isolation and purification of a target protein free of prion protein (prpSC).

Abstract: A process for manufacturing of a composition containing a purified factor for supporting wound healing selected from the group consisting of Hepatocyte Growth Factor (HGF) platelet derived growth factor (PDGF), Epidermal growth factor (EGF), transforming growth factor alfa (TGF-?), Transforming growth factor beta (TGF-?), insulin like growth factor (IGF-1) and Fibroblast growth factor (FGF) from sources, such as blood, containing the factor for supporting wound healing, wherein the manufacturing process comprises purification steps which are performed in the presence of antithrombin III (AT-III).

Abstract: The present invention provides a method for increasing the yield of a protein produced by cultivating eukaryotic cells and adding an ionic substance to the culture medium prior to harvest of the protein. Suitable ionic substances are the salts of the Hofmeister series, amino acids and peptone.

Abstract: Filtration methods comprise virus-filtering a solution containing a least one macromolecule. The total salt content of the solution for virus-filtering is within the range of from about 0.2 M up to saturation with the salt. Salts that can be used in the filtering methods include sodium chloride, potassium chloride, sodium acetate, sodium citrate, sodium phosphate, potassium dyhydrophosphate and combinations thereof.

Abstract: Filtration methods comprise virus-filtering a solution containing a least one macromolecule. The total salt content of the solution for virus-filtering is within the range of from about 0.2 M up to saturation with the salt. Salts that can be used in the filtering methods include sodium chloride, potassium chloride, sodium acetate, sodium citrate, sodium phosphate, potassium dyhydrophosphate and combinations thereof.

Abstract: The present invention relates to methods for purification of antithrombin-III (AT-III) by precipitation of impurities. The said methods comprise (a) adding, to a solution comprising antithrombin-III, a saccharide and citrate, in an amount sufficient for impurities to precipitate while antithrombin-III essentially remains in solution; (b) allowing impurities to precipitate; and (c) removing the precipitated impurities, thereby obtaining a solution comprising purified antithrombin-III. The invention also relates to pharmaceutical compositions, obtainable by the said methods, comprising purified antithrombin-III, as well as to reconstituted pharmaceutical compositions essentially free from visible particles.

Abstract: The present invention relates to methods for purification of antithrombin-III (AT-III) by precipitation of impurities. The said methods comprise (a) adding, to a solution comprising antithrombin-III, a saccharide and citrate, in an amount sufficient for impurities to precipitate while antithrombin-III essentially remains in solution; (b) allowing impurities to precipitate; and (c) removing the precipitated impurities, thereby obtaining a solution comprising purified antithrombin-III. The invention also relates to pharmaceutical compositions, obtainable by the said methods, comprising purified antithrombin-III, as well as to reconstituted pharmaceutical compositions essentially free from visible particles.

Abstract: Filtration methods comprise virus-filtering a solution containing a least one macromolecule. In one embodiment, the total salt content of the solution is within the range of from about 0.2 M to 2 M. In another embodiment, the total salt content of the solution is within the range of from about 0.2 M up to saturation with a salt, and the salt is selected from the group consisting of sodium chloride, potassium chloride, sodium acetate, sodium citrate, sodium phosphate, potassium dyhydrophosphate and combinations thereof. In yet another embodiment, the total salt content of the solution is within the range of from about 0.2 M up to saturation with the salt and the macromolecule is in solution during the virus filtering.

Abstract: PROTEIN PURIFICATION I The invention relates to processes for preparation of substantially pure antithrombin-III (AT-III), the antithrombin isoforms AT-III&agr; and AT-III&bgr;; and/or histidine-rich glycoprotein (HRGP). The processes comprise separating the said proteins on a cation exchange gel wherein the cation exchanger group is attached to the gel matrix via a linear polymer chain.

Abstract: The present invention relates to a process for purifying apolipoprotein A (ApoA) or apolipoprotein E (ApoE) from human plasma, by obtaining a fraction of human plasma containing said ApoA or ApoE, prepurifying said fraction in at least one step, binding said ApoA or ApoE to an anion-exchange chromatography gel, and thereafter eluting said ApoA or ApoE from said anion-exchange chromatography gel. The thus produced ApoA or ApoE can be used for the manufacture of a medicament in the treatment of atherosclerosis and cardiovascular diseases, or peripheral atherosclerosis and sepsis as well as in a method for treatment of atherosclerosis and cardiovascular diseases, or peripheral atherosclerosis and sepsis when administered in a therapeutically effective amount.

Abstract: Filtration methods comprise virus-filtering a solution containing at least one macromolecule. The total salt content of the solution is within the range of from about 0.2M to 2M or within the range of from about 0.2M up to saturation with the salt.

Abstract: PROTEIN PURIFICATION I

Abstract: The present invention relates to a process for purifying apolipoprotein A (ApoA) or apolipoprotein E (ApoE) from human plasma, by obtaining a fraction of human plasma containing said ApoA or ApoE, prepurifying said fraction in at least one step, binding said ApoA or ApoE to an anion-exchange chromatography gel, and thereafter eluting said ApoA or ApoE from said anion-exchange chromatography gel. The thus produced ApoA or ApoE can be used for the manufacture of a medicament in the treatment of atherosclerosis and cardiovascular diseases, or peripheral atherosclerosis and sepsis as well as in a method for treatment of atherosderosis and cardiovascular diseases, or peripheral atherosclerosis and sepsis when administered in a therapeutically effective amount.

Abstract: Virus inactivating chemicals and/or detergents in an aqueous composition containing a water-soluble plasma protein are reduced by selecting a suitable combination of temperature and concentration above 0.5M of salt with a high salting out effect according to the Hofmeister series, thereby forming vesicles containing the virus inactivating chemical and/or detergent. These vesicles are removed from the aqueous phase, e.g. by phase separation or filtration, and the protein thereafter isolated from the aqueous phase. The water-soluble plasma protein can be e.g. antithrombin III, transferrin or albumin. When the aqueous phase comprises e.g. a salt of citrate or sulphate in a concentration above 1M at room temperature, the reduction of virus inactivating chemical or detergent can be as high as 2000 times or more, giving a final concentration below 5 ppm.