Abstract: A process for purifying fibrinogen from a fibrinogen containing source by precipitation of fibrinogen by a precipitating agent from a fibrinogen containing solution in the presence of one or more chelating agent(s) and removal of the supernatant from the fibrinogen paste, characterised in that fibrinogen is extracted from the paste forming a liquid fraction containing fibrinogen, and an undissolved residue, which is separated from the liquid.

Abstract: A process for purifying fibrinogen from a fibrinogen containing source by precipitation of fibrinogen by a precipitating agent from a fibrinogen containing solution in the presence of one or more chelating agent(s) and removal of the supernatant from the fibrinogen paste, characterised in that fibrinogen is extracted from the paste forming a liquid fraction containing fibrinogen, and an undissolved residue, which is separated from the liquid.

Abstract: A process for purifying fibrinogen from a fibrinogen containing source by precipitation of fibrinogen by a precipitating agent from a fibrinogen containing solution in the presence of one or more chelating agent(s) and removal of the supernatant from the fibrinogen paste, characterized in that fibrinogen is extracted from the paste forming a liquid fraction containing fibrinogen, and an undissolved residue, which is separated from the liquid.

Abstract: A non-hemolytic acidic composition comprising an immunoglobulin selected from immunoglobulin A, immunoglobulin G or immunoglobulin M at a pH value in the range of 4.65 to 5.7 comprising one or more excipients selected from amino acids, sugars and sugar alcohols in a concentration range of 100-350 mmol/l, in particular 200-350 mmol/l, characterized in that it displays an optical density (OD) in the range of 0.14 to ?0.1 when the OD is determined in a spectrophotometer at 414 nm at a film thickness of 0.825 mm; and its use in an assay for determination of the hemolytic potential of intravenously applied pharmaceuticals and compositions and preparations displaying a reduced potential of hemolysis when being applied intravenously.

Abstract: A method for determining the likelihood of response of an individual, suffering from a disease, towards immunoglobulin therapy has the steps of providing a sample containing B- and T-lymphocytes, natural killer cells, invariant T-cells and monocytes of the individual; genotyping of at least one of the polynucleotides of an ADAMTS9-Intron; a KLHDC8A-Intron or of a flanking region of the CD14 gene, and awarding the value of 1 for the homozygous Single Nucleotide Polymorphism combinations, which suggests that the blood sample stems from a person which will not respond to immunoglobulin treatment, while awarding the value of 0 for SNP not meeting that criteria, which suggests that the blood sample stems from a person which will respond to immunoglobulin treatment.

Abstract: A process for purifying fibrinogen from a fibrinogen containing source by precipitation of fibrinogen by a precipitating agent from a fibrinogen containing solution in the presence of one or more chelating agent(s) and removal of the supernatant from the fibrinogen paste, characterised in that fibrinogen is extracted from the paste forming a liquid fraction containing fibrinogen, and an undissolved residue, which is separated from the liquid.

Abstract: A method for purification of complement Factor H from a complement Factor H containing source such as blood or blood plasma, in particular a caprylate precipitate of a Factor H containing source, which is e.g. obtained by addition of caprylate ions to fractions of blood or plasma, comprising the steps of: a) providing a Factor H containing source, in particular reconstitution of caprylate precipitate to provide a complement Factor H containing solution; b) performing a cation exchange chromatography in particular as first chromatographic step; c) performing an anion exchange chromatography; d) performing a hydroxyl apatite chromatography; e) followed by ultra/diafiltration to obtain a complement Factor H concentrate.

Abstract: A method for purification of complement Factor H from a complement Factor H containing source such as blood or blood plasma, in particular a caprylate precipitate of a Factor H containing source, which is e.g. obtained by addition of caprylate ions to fractions of blood or plasma, comprising the steps of: a) providing a Factor H containing source, in particular reconstitution of caprylate precipitate to provide a complement Factor H containing solution; b) performing a cation exchange chromatography in particular as first chromatographic step; c) performing an anion exchange chromatography; d) performing a hydroxyl apatite chromatography; e) followed by ultra/diafiltration to obtain a complement Factor H concentrate.

Abstract: Process for the stabilization of blood plasma components in a lyophilizate, wherein in a freeze-drying process, said blood plasma components were in a solution containing at least two different pH-lowering substances causing a predetermined pH value range to be adjusted in the solution formed upon reconstitution.

Abstract: A method for purification of complement Factor H from a complement Factor H containing source such as blood or blood plasma, in particular a caprylate precipitate of a Factor H containing source, which is e.g. obtained by addition of caprylate ions to fractions of blood or plasma, comprising the steps of: a) providing a Factor H containing source, in particular reconstitution of caprylate precipitate to provide a complement Factor H containing solution; b) performing a cation exchange chromatography in particular as first chromatographic step; c) performing an anion exchange chromatography; d) performing a hydroxyl apatite chromatography; e) followed by ultra/diafiltration to obtain a complement Factor H concentrate.

Abstract: A blood plasma for human use pooled from donors which belong to 10% or more to a non-Caucasian population, the plasma obtainable by mixing blood or blood plasma of blood groups A and B, optionally AB without admixing substantial amounts of blood or blood plasma of blood group 0 characterized in that four to eight parts of blood or blood plasma from donors having the blood group A, more than three parts to seven parts of blood or blood plasma from donors having the blood group B, zero to two parts of blood or blood plasma from donors having the blood group AB.

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 method of determining a patient's susceptibility for NK cell modulation by immunoglobulins in response to a treatment of a disease or prophylaxis of a disease with immunoglobulins wherein a modulation of natural killer cells caused by said immunoglobulins is determined.

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: Process for the stabilization of blood plasma components in a lyophilizate, wherein in a freeze-drying process, said blood plasma components were in a solution containing at least two different pH-lowering substances causing a predetermined pH value range to be adjusted in the solution formed upon reconstitution.

Abstract: A method of preparing a purified, virus inactivated and virus safe antibody preparation from a starting solution comprising antibodies and contaminants, the method comprising the steps of: (a) adjusting the pH of the starting solution to about 4.6 to about 4.95 in particular to about 4.8 to about 4.95 to produce an intermediate solution; (b) adding caprylate and/or heptanoate ions to the intermediate solution and maintaining the pH at about 4.6 to about 4.95 in particular pH at about 4.8 to about 4.

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.