Octapharma Ag

Biovitrum Ab

Esperion Therapeutics, Inc.

Pharmacia & Upjohn Aktiebolag

Stefan Winge

Christoph Kannicht

Gustav Gilljam

Gerhard Gruber

Guido Kohla

Barbara Solecka-Witulska

Maya Tiemeyer

Sara Wiklund

Mats Jernberg

Andrea Neisser-Svae

Ulrika Ericsson

Barbara Solecka

Sven Isaksson

Carin Borgvall

Birte Fuchs

Tilo Schwientek

Alex Scheepers

Per Rosen

Marina Dadaian

Erica Johansson

Anna Mjärdestam

Frederic Bal

Petra Schultz

Frank Marks

The invention relates to a fusion protein comprising a main protein and one or more extension peptides, wherein the amino acid sequence of the main protein is identical or similar to the amino acid sequence of a mammalian protein or a fragment thereof, and said extension peptide comprises a cluster of O-glycosylated amino acids. The extension peptide is identical to a non-repeated sequence of the mammalian protein and/or identical or similar to SEQ ID NO: 1. The main protein is preferably VWF. The fusion protein has an increased half life as compared to the main protein and may be used to increase the half-life of a binding partner, e.g. FVIII. The invention further relates to the complex formed by the fusion protein, a polynucleotide encoding the fusion protein as well as a vector and host cell comprising the polynucleotide.

Glycosylated VWF fusion proteins with improved pharmacokinetics

The invention relates to a glycosylated polypeptide comprising an amino acid sequence being identical or homologous to at least a fragment of a mammalian, preferably a human protein, wherein said glycosylated polypeptide contains one or more sialylated O-glycans and wherein the glycosylated polypeptide shows an increased binding affinity to one or more SIGLECs, selected from SIG-5, SIG-7, SIG-8, and SIG-9 compared to the mammalian protein or fragment thereof. The invention further relates to composition comprising a first and a second polypeptide, wherein the first polypeptide is a glycosylated polypeptide containing one or more sialylated O-glycans and the second polypeptide contains an amino acid sequence homologous or identical to a second mammalian, in particular human protein, wherein compared to the second polypeptide the composition has an increased binding affinity to a SIGLEC selected from to one or more SIGLECs, selected from SIG-5, SIG-7, SIG-8, and SIG-9.

Polypeptides modulating SIGLEC dependent immune responses

The invention provides a method for separating a Factor VIII (FVIII) protein from a first composition comprising the FVIII protein, which contains at least the light chain of FVIII, and a von-Willebrand-Factor (vWF) protein which comprises at least the FVIII binding domain of vWF, wherein the FVIII protein can form a complex with the vWF protein, the method comprising the steps: contacting the first composition with an affinity resin comprising a ligand and a matrix, wherein the ligand has an affinity to the light chain of FVIII, and separating the affinity resin from the mixture to obtain a modified first composition and a second composition, wherein the second composition contains the affinity resin, and a complex of the FVIII protein and the vWF protein.

Method of separating Factor VIII from blood products

A process for manufacturing of a Factor VIII product having a ratio of FVIII:C/FVIII:Ag of at least 0.7 in the Factor VIII product by using chromatography wherein at least one chromatographic step is performed by means of employing; An affinity chromatography resin having an affinity for specifically binding of Factor VIII which is effected by an affinity ligand which is immobilised on the affinity chromatography resin, said affinity ligand is a 13 kD yeast derived Fab antibody fragment directed to the Factor VIII molecule. An anionic chromatography resin. A size exclusion resin. A Factor VIII product obtainable according to the process with a monomer content of &#x3e;98% for treatment of haemophilia and avoiding formation of inhibitors.

Process for manufacturing factor VIII having an improved ratio of FVIII:C/FVIII/AG

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.

Method for improved isolation of recombinantly produced proteins

A composition comprising a complex of Factor VIII and one or more Von Willebrand Factor peptides, wherein the Von Willebrand Factor peptides comprise at least the amino acids 764 to 1035 and 1691 to 1905 of SEQ ID No. 1 but not amino acids 2255 to 2645 of SEQ ID No. 1.

Preparation comprising factor VIII and Von Willebrand factor peptides

A method of purifying a Growth Factor Protein in a purification sequence employing chromatography is provided. The method comprises performing at least one chromatography step using a multimodal resin, binding the Growth Factor Protein to the multimodal resin at a pH from 4 to 6.2, and eluting the Growth Factor Protein at a pH in the range of from 5.5 to 6.5. The elution of Growth Factor Protein is improved by addition of arginine and/or NaCl in the eluting buffer. Optionally the multimodal resin step is followed by a yeast derived affinity ligand resin step, which results in a purity of the product greater than 90%.

Process for the purification of a growth factor protein

A process of purifying the Growth Factor Protein G-CSF (Granulocyte Colony Stimulating Factor) in a purification sequence employing chromatography, comprising binding the G-CSF to Capto MMC&#x2122;, which is a multimodal resin that comprises a negatively charged 2-(benzoylamino) butanoic acid ligand, at a pH from 4 to 6.2; and eluting the G-CSF at a pH greater than 6.3.

A process for isolation and purification of a target protein by chromatography wherein the chromatography removes or depletes prions (PrP), comprising the steps of contacting a potentially PrPcontaminated 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 PrPis 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 (prp).

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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-&#x3b1;), Transforming growth factor beta (TGF-&#x3b2;), insulin like growth factor (IGF-I) 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).

Purification and use of a factor for supporting wound healing

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.

Process of purifying coagulation factor VIII

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.

Method for purification of proteins

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.

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Arsta, Sweden

Stefan Winge