Abstract: The invention relates to compositions comprising an isolated sugar for use in the treatment of von Willebrand disease and/or hemophilia A, wherein the sugar is an accessible sugar residue derived from ABO(H) blood group antigen.

Abstract: The invention relates to compositions comprising an isolated sugar for use in the treatment of von Willebrand disease and/or hemophilia A, wherein the sugar is an accessible sugar residue derived from ABO(H) blood group antigen.

Abstract: The invention relates to compositions comprising an isolated sugar for use in the treatment of von Willebrand disease and/or hemophilia A, wherein the sugar is an accessible sugar residue derived from ABO(H) blood group antigen.

Abstract: The invention relates to compositions comprising an isolated sugar for use in the treatment of von Willebrand disease and/or hemophilia A, wherein the sugar is an accessible sugar residue derived from ABO(H) blood group antigen.

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: 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: 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 procedure for the determination of the activity of the protease which activates blood clotting factor VII from protein solutions is describes, in which the protein solution comprising the protease and/or its proenzyme is incubated with a solid phase to which an antibody which binds the protease and/or its proenzyme has been coupled beforehand, and after washing the solid phase, the protease and/or its proenzyme fixed thereto, are incubated with reagents which allow for the determination of their activity.

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 novel 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: A stabilized liquid preparation of a protease which activates blood coagulation Factor VII or of its proenzyme is herein described. The preparation also contains one or more compounds selected from the group consisting of ornithine, diaminopimelic acid, agmatine, creatine, guanidinoacetic acid, acetylornithine, citrulline, arginoinosuccinic acid, tranexamic acid and epsilon-aminocaproic acid or their salts and has a pH of 2–8.

Abstract: A novel 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: A protease for activating the blood clotting factor VII is described, wherein the protease is inhibited by the presence of aprotinin and is increased in its activity by calcium ions and/or heparin or heparin-related substances, and wherein in SDS-PAGE, on subsequent staining in the non-reduced state, the protease has one or more brands in the molecular weight range from 50 to 75 kDa, and in the reduced state, the protease has a band at 40 to 55 kDa and one or more bands in the molecular weight range from 10 to 35 kDa. The proenzyme of this protease is also characterized. Further, a process for obtaining this protease and its use in hemorrhage prophylaxis or hemostasis is described. Moreover, a test system for the qualitative and quantitative detection of a protease which activates the blood clotting factor VII is described.

Abstract: Mutants of the DNA sequence coding for the protease (FSAP) which activates blood clotting factor VII and single-chain plasminogen activators, the mutant comprising a G/C base exchange at nucleotide position 1177 and/or a G/A base exchange at nucleotide position 1601, is 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. Furthermore, 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 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: 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 process for the preparation in pure form of the protease activating blood clotting factor VII and/or its proenzyme is described in which these are obtained from biological fluids or those obtained in the case of preparation by genetic engineering

Abstract: A stabilized protein preparation is described which contains no antithrombin III and is protected against loss of activity during pasteurization by the addition of stabilizers which comprise one or more saccharides as a mixture with more than 0.5 mol/l of one or more amino acids chosen from the group arginine, lysine, histidine, phenylalanine, tryptophan, tyrosine, aspartic acid and its salts or glutamic acid and its salts. Glycine and/or glutamine can also be additionally added to each of these amino acids. A process for the viral inactivation or viral depletion of a protein preparation of this type which contains the abovementioned stabilizers and is subjected to pasteurization or viral depletion by filtration, centrifugation or treatment with detergents or bactericidal or virucidal agents is also described.