Abstract: There are disclosed a stable factor VIII/vWF-complex, particularly comprising high-molecular vWF multimers, being free from low-molecular vWF molecules and from proteolytic vWF degradation products, as well as a method of producing this complex.

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: A method for separation of recombinant pro-Factor IX from recombinant Factor IX by a chromatographic method is described. According to a preferred embodiment, the mixture of both proteins is bound to an ion exchanger and pro-Factor IX and Factor IX are eluted separately from each other by buffer solutions with different salt concentrations and/or pH values.According to the method of the invention, pro-Factor IX and Factor IX are obtainable in highly pure form and free from the other factor respectively.

Abstract: There is disclosed the preparation and recovery of proteins, in particular of enzymes, by controlled proteolytic cleavage of pro-proteins, in particular pro-enzymes, in a single method step, wherein a pro-protein-containing solution is contacted with a protease and with a solid carrier which has a higher affinity to the protein than to the pro-protein or to the functionally inactive degradation products thereof, the pro-protein being proteolytically cleaved to said protein, and the protein being selectively separated by absorption on the solid carrier.

Abstract: The invention provides high and low molecular weight fraction of von Willebrand Factor (vWF), which can be obtained by absorbing vWF to a heparin affinity support followed by eluting the vWF at differing salt concentrations.

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 provides high and low molecular weight fraction of von Willebrand Factor (vWF), which can be obtained by absorbing vWF to a heparin affinity support followed by eluting the vWF at differing salt concentrations The low molecular weight fraction is predominantly dimers and tetramers, and the high molecular weight fraction is predominantly larger multimers.

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.

Abstract: A method for the separation of vitamin K-dependent proteins from non-vitamin K-dependent accompanying proteins is described wherein the method is characterized in that at least anion exchange chromatography and optionally affinity chromatography is carried out as well. The method is suitable especially for the purification of Factor II, VII, IX, X as well as Protein S, Protein C and Protein Z. With the aid of the method according to the invention a vitamin K-dependent protein is obtained which is present at a purity of 95%.

Abstract: There is disclosed a complex comprised of an insoluble polymer carrier to which monomeric human albumin is covalently bound and of a pre-S hepatitis B surface antigen bound in an elutable form to the monomeric human albumin by its pre-S(2)- and/or pre-S(1)-region. This complex may be used for therapeutic and diagnostic purposes and enables the rapid and efficient purification of pre-S-HBsAg by affinity chromatography.

Abstract: There is disclosed a complex comprised of an insoluble polymer carrier to which monomeric human albumin is covalently bound and of a pre-S hepatitis B surface antigen bound in an elutable form to the monomeric human albumin by its pre-S(2)- and/or pre-S(1)-region. This complex may be used for therapeutic and diagnostic purposes and enables the rapid and efficient purification of pre-S-HBsAg by affinity chromatography.

Abstract: There is disclosed a complex comprised of an insoluble polymer carrier to which monomeric human albumin is covalently bound and of a pre-S hepatitis B surface antigen bound in an elutable form to the monomeric human albumin by its pre-S(2)- and/or pre-S(1)-region. This complex may be used for therapeutic and diagnostic purposes and enables the rapid and efficient purification of pre-S-HBsAg by affinity chromatography.

Abstract: Polydisperse native Pseudomonas flagellar (H) antigens (FAg) and methods of producing them are described, wherein each monomeric component contains certain amino acids, has a certain N-terminal amino acid sequence and a certain molecular weight and is free from pyrogenic substances. The ratio of the individual amino acids in the flagellar antigen of the individual H-serotypes is stated.For producing the polydisperse native Pseudomonas flagellar (H) antigens (FAg) methods are indicated, wherein Pseudomonas aeruginosa bacterial cultures or fractions thereof are treated with a detergent and the flagellar antigens are separated from the cultures. Prior to treatment or in the presence of the detergent, the bacterial culture is subjected to a shearing procedure, i.e. exposed to shearing forces. Thereafter, the flagellar antigens separated from the bacterial mass are isolated by a chromatographic treatment.