Abstract: Nucleic acids encoding factor X analogues are provided that have a modification in the region of the natural Factor Xa activation cleavage site. The modification results in a processing site for a protease not naturally cleaving in this region of the Factor X sequence.

Abstract: This invention describes a factor Xa analog which has a substitution of a minimum of one of the amino acid between Glu226 and Arg234 and possibly Ile235, relative to the amino acid numbering according to FIG. 1, a preparation containing the activated form of the factor X analog, and a method for the production of these molecules.

Abstract: Nucleic acids encoding factor X? analogues having a deletion of amino acids Arg180 to Arg234 and a modification in the region of the amino acid sequence between Gly173 and Arg 179 are provided.

Abstract: Factor X analogues having a modification in the region of the natural Factor Xa activation cleavage site, said modification representing a processing site of a protease not naturally cleaving in this region of the Factor X sequence, preparations containing the Factor X analogues according to the invention, and processes for the preparation thereof are described.

Abstract: Factor X&Dgr; analogues having a deletion of amino acids Arg180 to Arg234 and a modification in the region of the amino acid sequence between Gly173 and Arg179, preparations containing these factor X&Dgr; analogues, and processes for the preparation thereof are described.

Abstract: The present invention comprises a furin polypeptide having a modified amino acid sequence between the middle, homo-B-domain and the transmembrane domain compared to wild-type furin which retains proteolytic activity but is secreted at lower levels in cell culture compared to wild-type furin. Additionally, the invention includes nucleic acid molecules encoding such furin polypeptides, vectors and host cells comprising said nucleic acid molecules, compositions comprising said furin polypeptide and methods for producing such compositions.

Abstract: Factor X analogues having a modification in the region of the natural Factor Xa activation cleavage site, said modification representing a processing site of a protease not naturally cleaving in this region of the Factor X sequence, preparations containing the Factor X analogues according to the invention, and processes for the preparation thereof are described.

Abstract: Factor X&Dgr; analogues are provided, as well as pharmaceutical preparations containing such analogues and methods of preparing such analogues. The factor X&Dgr; analogues have a deletion of the amino acids Arg180 to Arg234 and a modification in the region of the amino acid sequence between Gly173 and Arg179 of the factor X amino acid sequence. Such analogues can include a processing site not normally present in factor X, thus allowing for selective conversion of the analogue to an active form. The analogues and preparations have utility in the treatment of a number of blood coagulation disorders.

Abstract: Fusion proteins of an optionally C-terminally deleted furin derivative, or of a derivative of a furin analogue, and a heterologous sequence, methods of preparing the same and methods of recovering proproteins from proteins by using the proproteins according to the invention are described.

Abstract: The invention describes an expression plasmid containing a dicistronic transcription/translation unit, which unit comprises a sequence for a foreign protein and a sequence for a fusion protein, the fusion protein containing at least one selection marker and at least one amplification marker. Further described is a method of producing foreign proteins by using the plasmids according to the invention, as well as cell lines transformed with the plasmid according to the invention.

Abstract: The invention relates to a method for isolation of highly pure von Willebrand Factor in which recombinant von Willebrand Factor (rvWF) is chromatographically purified by anion exchange chromatography on an anion exchanger of the quaternary amino type in a buffer solution comprising buffer substances and optionally salt.The buffer solutions are preferably free of stabilizers, amino acids and other additives. According to this method, highly pure recombinant vWF can be obtained, which is free from blood plasma proteins, especially free from Factor VIII, and is physiologically active.Further, the invention relates to a pharmaceutical preparation that contains rvWF, which is comprised of multimers with a high structural integrity.

Abstract: The invention relates to new prothrombin mutants or derivatives thereof which comprise one or more changes in their protein sequence as compared to natural protein, are either inactive or have an activity of approximately 10% at the most, preferably approximately 0.25% at the most, of the natural protein and which have a binding capacity relative to natural ligands (natural or synthetic anticoagulants) substantially corresponding to that of the natural protein. Furthermore, the use of mutated prothrombin mutants or derivatives, respectively, as pharmaceutical preparations is described.

Abstract: The invention relates to a method for isolation of highly pure von Willebrand Factor in which recombinant von Willebrand Factor (rvWF) is chromatographically purified by anion exchange chromatography on an anion exchanger of the quaternary amino type in a buffer solution comprising buffer substances and optionally salt.The buffer solutions are preferably free of stabilizers, amino acids and other additives. According to this method, highly pure recombinant vWF can be obtained, which is free from blood plasma proteins, especially free from Factor VIII, and is physiologically active.Further, the invention relates to a pharmaceutical preparation that contains rvWF, which is comprised of multimers with a high structural integrity.

Abstract: The invention relates to a method for isolation of highly pure von Willebrand Factor in which recombinant von Willebrand Factor (rvWF) is chromatographically purified by anion exchange chromatography on an anion exchanger of the quaternary amino type in a buffer solution comprising buffer substances and optionally salt.The buffer solutions are preferably free of stabilizers, amino acids and other additives. According to this method, highly pure recombinant vWF can be obtained, which is free from blood plasma proteins, especially free from Factor VIII, and is physiologically active.

Abstract: The invention relates to a method for isolation of highly pure von Willebrand Factor in which recombinant von Willebrand Factor (rvWF) is chromatographically purified by anion exchange chromatography on an anion exchanger of the quaternary amino type in a buffer solution comprising buffer substances and optionally salt. The buffer solutions are preferably free of stabilizers, amino acids and other additives. According to this method, highly pure recombinant rvWF can be obtained, which is free from blood plasma proteins, especially free from Factor VIII, and is physiologically active. Further, the invention relates to a pharmaceutical preparation that contains rvWF, which comprises mulitimers with a high structural integrity.