Abstract: A process of freeze drying of an essentially aqueous solution comprising at least one first step having a first temperature and pressure level (i.e. primary drying phase) and at least one second step having a second temperature and pressure level (i.e. secondary drying phase) following the first step, wherein in the secondary drying phase limited desorption energy input is applied.

Abstract: A G-CSF precursor comprising a signal peptide and a G-CSF peptide, wherein the signal peptide has the sequence of the human wild-type signal peptide of the human G-CSF/b molecule with at least one of the following mutations: deletion of Glu29, insertion of Glu26, substitution Lys11Leu, substitution His21Phe, and substitution Gln28Leu.

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 for preparing a hemostatically active preparation containing von Willebrand factor (vWF) from a fraction of human plasma by chromatographic purification of a vWF-containing plasma fraction on an anion-exchange material which has the anion-exchanging groups on grafted polymeric structures (tentacle materials), collecting a vWF-containing fraction, followed by purification of said fraction using gel permeation to prepare a purified thermally stable vWF-containing preparation; and heating the preparation for inactivating viruses.

Abstract: The present invention relates to an improved method for the serum-free production of an immortalized human cell line stably transfected under serum-free conditions with a specific vector carrying the gene coding for the protein of interest. Furthermore the invention relates to a production cell line obtained by said method, a production method for said protein of interest utilizing said production cell line, and the specific vector carrying the gene of interest itself.

Abstract: An albumin containing fraction having a reduced prekallikrein activator (PKA) content and a method of manufacturing same comprising the steps of: (a) reconstitution of paste V (Cohn fractionation), (b) performing a concentration step of the fraction obtained in step (a), (c) heating the fraction obtained in step (b) in a range of from 50° C. to 70° C. for a sufficient time to pasteurize the fraction, and (d) optionally filling of the obtained fraction for use.

Abstract: A method of preparing a purified, virus inactivated and virus safe antibody preparation from a starting solution comprising antibodies and contaminants, the method comprising the steps of: (a) adjusting the pH of the starting solution to about 4.6 to about 4.95 in particular to about 4.8 to about 4.95 to produce an intermediate solution; (b) adding caprylate and/or heptanoate ions to the intermediate solution and maintaining the pH at about 4.6 to about 4.95 in particular pH at about 4.8 to about 4.

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: A process of freeze drying of an essentially aqueous solution comprising at least one first step having a first temperature and pressure level (i.e. primary drying phase) and at least one second step having a second temperature and pressure level (i.e. secondary drying phase) following the first step, wherein in the secondary drying phase limited desorption energy input is applied.

Abstract: A method of preparing a purified, virus inactivated and virus safe antibody preparation from a starting solution comprising antibodies and contaminants, the method comprising the steps of: (a) adjusting the pH of the starting solution to about 4.6 to about 4.95 in particular to about 4.8 to about 4.95 to produce an intermediate solution; (b) adding caprylate and/or heptanoate ions to the intermediate solution and maintaining the pH at about 4.6 to about 4.95 in particular pH at about 4.8 to about 4.

Abstract: A process for preparing a hemostatically active preparation containing von Willebrand factor (vWF) from a fraction of human plasma by chromatographic purification of a vWF-containing plasma fraction on an anion-exchange material which has the anion-exchanging groups on grafted polymeric structures (tentacle materials), collecting a vWF-containing fraction, followed by purification of said fraction using gel permeation to prepare a purified thermally stable vWF-containing preparation; and heating the preparation for inactivating viruses.

Abstract: A process for preparing A1AT from A1AT-containing solutions, comprising the following steps: (a) subjecting an A1AT-containing solution to ion-exchange chromatography; (b) adding detergents and optionally a solvent for inactivating lipid-enveloped viruses; (c) followed by increasing the salt concentration to salt out the detergents. A1AT having a purity of >90% with an activity of ?0.8 PEU/mg in its active form.

Abstract: Disclosed is a process for preparing agents containing virus-inactivated vitamin K-dependent plasma components as well as protein C, protein S, factors II, VII, IX and/or X as well as combinations thereof, such as, for example, PPSB preparations, wherein a source containing these components is subjected to a appropriate separation procedures, especially by using membrane-chromatographic methods.

Abstract: The present invention relates to a process for the preparation of a solution comprising a substantially pure isoform of AT-III, said process comprising separating the isoform AT-III&agr; from AT-III&bgr; on a calcium hydroxyphosphate-based adsorbent.

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: A method for the inactivation of viruses, in particular those having no lipid coats, in protein-containing compositions from blood, blood plasma or similar natural sources by treating said source, simultaneously or succesively, with an effective amount of dialkyl or trialkyl phosphates and optionally surfactants at an elevated temperature in the range of from 55° C. to 67° C. for five hours to 30 hours.

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: Disclosed is a process for preparing agents containing virus-inactivated vitamin K-dependent plasma components as well as protein C, protein S, factors II, VII, IX and/or X as well as combinations thereof, such as, for example, PPSB preparations, wherein a source containing these components is subjected to a appropriate separation procedures, especially by using membrane-chromatographic methods.