Abstract: The production of a thrombin preparation which is obtained from prothrombin which is, after activation to thrombin without the addition of thromboplastin, purified by a hydrophobic interaction chromatography, it being possible subsequently also to inactivate or remove viruses, is described. Before or after the hydrophobic interaction chromatography it is also possible in addition to carry out a cation exchange chromatography. A thrombin preparation which contains as stabilizer a noncovalently binding inhibitor and to which further stabilizers can be added for stabilization in the liquid state is additionally described.

Abstract: The invention relates to a method for determining a factor XIII deficiency, a method for determining a fibrinogen deficiency, and a method for differentiating between a factor XIII deficiency and a fibrinogen deficiency by means of thrombelastographic techniques. On the basis of the evaluation of the thrombelastographic parameters, a rapid and a selective substitution of factor XIII and/or of fibrinogen in deficiency states is possible.

Abstract: The invention relates to therapeutic fusion proteins in which a coagulation factor is fused to a half-life enhancing polypeptide, and in which both are connected by a linker peptide that is proteolytically cleavable. The cleavage of such linkers liberates the coagulation factor from activity-compromising steric hindrance caused by the half-life enhancing polypeptide and thereby allows the generation of fusion proteins may show relatively high molar specific activity when tested in coagulation-related assays. Furthermore, the fact that the linker is cleavable can enhance the rates of inactivation and/or elimination after proteolytic cleavage of the peptide linker compared to the rates measured for corresponding therapeutic fusion proteins linked by the non-cleavable linker having the amino acid sequence GGGGGGV.

Abstract: The present application relates to procedures for the determination of the activity of the protease which activates factor VII, also known as factor VII activating protease or FSAP. The application also relates to a method of detecting whether an individual has increased or lowered activity in the protease which activates factor VII compared to at least one standard sample, wherein the increased or lowered activity indicates an increased risk for disease or cardiovascular complications.

Abstract: This application describes methods of treatment involving a protease for activating the blood clotting factor VII, which (a) activates blood clotting factor VII, (b) is inhibited by the presence of aprotinin, (c) is increased in its activity by the presence of at least one of the following: calcium ions, heparin, or heparin related substances, and (d) in SDS-PAGE, on subsequent staining in the non-reduced state, has one or more bands in the molecular weight range from 50 to 75 kDa, and in the reduced state has a band at 40 to 55 kDa and one or more bands in the molecular weight range from 10 to 35 kDa, and a band, which corresponds to a proenzyme, in the molecular weight range from 60 to 65 kDa.

Abstract: This application includes description of antibodies for specifically detecting prions of human origin and methods for detecting pathogenic prions. In some embodiments, the antibodies bind to an epitope characteristic of a human prion protein which is not found in the prion proteins of other species. In some embodiments, the antibodies are not cross-reactive with cow, Syrian Gold hamster, mouse, or rat prions. The application also includes a conformation-dependent immunoassay method for detecting pathogenic prions in a sample containing a prion (PrP) protein. The PrP protein may be present in a first conformation and a second conformation, such as PrPc and PrPSc in which the two conformations have different binding affinity for the antibody used to detect them.

Abstract: Mutants of the DNA sequence coding for the protease (FSAP) which activates blood clotting factor VII and single-chain plasminogen activators, the mutants comprising a G/C base exchange at nucleotide position 1177 and/or a G/A base exchange at nucleotide position 1601, are described. The corresponding protease has a Glu/Gln exchange at amino acid position 393 and/or a Gly/Glu exchange at amino acid position 534. Diagnostic methods which are used for detecting FSAP in body fluids or tissue cells and also for identifying patients with genetic heterozygous or homozygous FSAP expression are also described. In addition, antibodies against FSAP and its mutants are disclosed and diagnostic methods which can be used to detect antibodies against FSAP and its mutants are specified.

Abstract: A monoclonal antibody which inhibits the blood clotting factor VII-activating protease and its proenzyme and a blood clotting factor VII-activating protease, stabilized by the addition of said monoclonal antibody, and its proenzyme are described. A suitable monoclonal antibody is produced by hybridoma cell line DSM ACC 2533. The application of the inhibitory, monoclonal antibody in the stabilization of blood clotting preparations and in preparations for reducing the coagulability of the blood is disclosed.

Abstract: An arterial thrombosis risk factor comprising one or more of the identified mutants of coagulation factor VII activating protease (FSAP) is described. In addition, diagnostic determination methods for detecting these mutants which are identified as risk factors are described.

Abstract: The invention relates to a concentrate and a process for producing a factor VIII:C-containing von Willebrand factor by fractional precipitation from a liquid comprising factor VIII:C and von Willebrand factor, resulting in an increased content of high molecular weight multimers of von Willebrand factor and a ratio of the vWF:RCoF activity to vWF:Ag of greater than 1.

Abstract: The invention relates to a flowable fibrin adhesive granulate containing thrombin, Factor XIII, fibrinogen, and a calcium salt in the form of granules with a particle size of more than 50 ?m to 1000 ?m. Said granulate is useful for the healing of wounds in surgery, tissue therapy and/or as supporting material for biological factors. The invention also relates to an effervescent granulate and an effervescent powder for producing a foam that is suitable for hemostasis. The invention further relates to preparations to arrest bleeding containing a non-woven fabric for wounds consisting of a biodegradable supporting material that is coated with a fibrin glue granulate mixture or mixed granulate.

Abstract: The present invention relates to a process for purifying fibrinogen, which comprises one or more process steps in which one or more contaminating proteins are depleted by negative chromatography and/or negative adsorption using cation exchanger, hydrophobic gel and/or dye gel. In addition, the invention relates to the fibrinogen which is obtained by the process of the invention and which is notable for improved stability, and to the production and use of pharmaceutical preparations comprising this fibrinogen.

Abstract: The present invention relates to modified cDNA sequences coding for vitamin K-dependent polypeptides, in particular human Factor VII, human Factor VIIa, human Factor IX and human protein C and their derivatives with improved stability and extended plasma half life, recombinant expression vectors containing such cDNA sequences, host cells transformed with such recombinant expression vectors, recombinant polypeptides and derivatives which do have biological activities of the unmodified wild type protein but having improved stability and processes for the manufacture of such recombinant proteins and their derivatives. The invention also covers a transfer vector for use in human gene therapy, which comprises such modified DNA sequences.

Abstract: Embodiments of the invention include a fluid transfer device, for example, for medical fluids. The device includes a housing, two piercing elements mounted in the housing, and a slide arranged between the piercing elements. The slide may be displaced with respect to the piercing elements such that, in a first position, a flow connection is established between the two piercing elements, and, in a second position, a flow connection is established between one of the piercing elements and a lateral opening of the housing. In the area of the lateral opening, the housing may have a connector for insertion of a syringe cone of a syringe. When the syringe cone is inserted into the connector, the front end of the syringe cone may move the slide from the first position to the second position.

Abstract: Mutants of the DNA sequence coding for the protease (FSAP) which activates blood clotting factor VII and single-chain plasminogen activators, the mutants comprising a G/C base exchange at nucleotide position 1177 and/or a G/A base exchange at nucleotide position 1601, are described. The corresponding protease has a Glu/Gln exchange at amino acid position 393 and/or a Gly/Glu exchange at amino acid position 534. Diagnostic methods which are used for detecting FSAP in body fluids or tissue cells and also for identifying patients with genetic heterozygous or homozygous FSAP expression are also described. In addition, antibodies against FSAP and its mutants are disclosed and diagnostic methods which can be used to detect antibodies against FSAP and its mutants are specified.

Abstract: The production of a thrombin preparation which is obtained from prothrombin which is, after activation to thrombin without the addition of thromboplastin, purified by a hydrophobic interaction chromatography, it being possible subsequently also to inactivate or remove viruses, is described. Before or after the hydrophobic interaction chromatography it is also possible in addition to carry out a cation exchange chromatography. A thrombin preparation which contains as stabilizer a noncovalently binding inhibitor and to which further stabilizers can be added for stabilization in the liquid state is additionally described.

Abstract: Use of plasma proteins concentrates containing VWF with a high proportion of high molecular weight multimers prevents a bleeding diathesis and reduces pre-, peri- and postoperative blood loss in acquired Von Willebrand syndromes such as in cardiovascular diseases requiring surgical procedures, especially those requiring extracorporeal circulation.