Abstract: The gammaglobulin is extracted from a fraction isolated by fractionation with ethanol in the presence of a carbohydrate, and after reducing the content of contaminants with PEG, it is applied to an anionic resin exchange column, an effluent being obtained in which the PEG content is subsequently reduced by ultrafiltration and which is concentrated in order to carry out sequentially an optional treatment at an acid pH and at least one of the following steps of viral inactivation, consisting of pasteurisation and a treatment with solvent/detergent, the product afterwards being precipitated and washed with PEG in order to eliminate any chemical viral inactivation reagents and then, by solubilisation and change of pH, the protein contaminants, and finally purified by ultrafiltration to reduce the volume and the PEG content, then carrying out an optional virus filtration and subsequent concentration.

Abstract: The present application concerns concentrated protein formulations with reduced viscosity, which are particularly suitable for subcutaneous administration. The application further concerns a method for reducing the viscosity of concentrated protein formulations.

Abstract: A composition exhibiting reverse thermal gellation properties comprises a block polymer having the structure: {[An(BCB)An]}m wherein A is a polyester unit, B is a poly(ethylene oxide) unit, C is a poly(propylene oxide) unit, E is a chain extender unit, n=0-20, and m is greater than 2. The ethylene oxide:propylene oxide ratio ranges from about 0.2:1 to about 40:1. The composition has a final viscosity at a final temperature of more than twice the initial viscosity at an initial temperature wherein the final temperature is at least 10° C. higher than the initial temperature. The composition is combined with either a cellular material for tissue engineering, a cellular material for effecting repair or healing in a patient, or a bioactive agent.

Abstract: The invention relates to the field of protein purification and the recovery of large proteinaceous material through small, nanometer sized, pore exclusion filters for removal of contaminants such as viral pathogens.

Abstract: Methods are disclosed for sterilizing preparation of monoclonal immunoglobulins to reduce the level of active biological contaminants such as viruses, bacteria, yeasts, molds, mycoplasmas, prions and parasites.

Abstract: Method of reducing the anticomplement activity (ACA) resulting from viral inactivation treatment of a solution of antibodies, the method comprising contacting the solution with a trialkylphosphate, such as tri-n-butyl phosphate, and a detergent, such as sodium cholate, under conditions sufficient to reduce substantially the virus activity, and then incubating the solution under controlled conditions of time, pH, temperature, and ionic strength such that the anticomplement activity is reduced to an acceptable level. In a preferred embodiment, the ACA is reduced to less than 60 CH50 units/mL, the incubation is for at least about ten days at a pH from 3.5 to 5.0, the temperature is maintained within a range of 2 to 50° C., and the ionic strength of the solution is less than about 0.001 M.

Abstract: The F. necrophorum gene expressing leukotoxin was sequenced and cloned. The leukotoxin open reading frame (lktA) is part of a multi-gene operon containing 9,726 bp, and encoding a protein containing 3,241 amino acids with an overall molecular weight of 335,956 daltons. The protein encoded by the gene was truncated into five polypeptides having overlapping regions by truncating the full length gene into five different sections and amplifying, expressing, and recovering the protein encoded by each of these sections. Additionally, a region upstream of the gene was sequenced and the polypeptide encoded by that nucleotide sequence was purified and isolated. These polypeptides along with the full length protein are then tested to determine their immunogenicity and protective immunity in comparison to the efficacy of immunization conferred by inactivated native leukotoxin in F. necrophorum culture supernatant.

Abstract: A method for the separation of IgG and IgA from an immunoglobulin-containing starting material is described, whereby the method is characterized in that (i) IgG and optionally IgA are adsorbed to a solid inorganic carrier material, (ii) IgA is isolated from the eluate, optionally after selective desorption, whereas IgG remains on the carrier material, and optionally (iii) IgG is isolated from the adsorbate. Furthermore, an IgA preparation is disclosed which demonstrates a low tendency to form aggregates.

Abstract: Combinations of ACE inhibitors and vasopressin antagonists are useful to slow and reverse the process of ventricular dilation, and CHF in mammals.

Abstract: A method for treating a skin condition by intimately combining a water soluble antibiotic with the keratin layer of the outermost layer of the cleansed epidermis. The antibiotic is dissolved in the alkaline fraction of an electrolyzed water. The solution is characterized by the absence of hydrolysis products, turbidity, and loss of potency of the antibiotic. The aqueous solution is applied to the treatment area where the water is absorbed by the keratin and the antibiotic is carried into intimate contact with the keratin after which the water is evaporated leaving the antibiotic dispersed across the treatment area.

Abstract: Liposomal conjugates having a clinically useful delivery vehicle linked to a biologically active species which acts to increase vascular permeability and expand blood volume at or in proximity to the tumor site are disclosed. The vehicle-linked species may be, for example, a vasoactive agent, a substance that recruits or amplifies a vasoactive species, a drug, or a pharmaceutical compound. Suitable biological species comprises peptides, lipids, carbohydrates, or their derivatives. Chemical or recombinant DNA methods suitable for linking the species to the vehicles are indicated. A therapy is disclosed which comprises administering the vasoactive conjugate and delivering a diagnostic agent or a therapeutic agent at an optimal time thereafter, when tumor vasculature is maximally affected.

Abstract: A method for producing an immunoglobulin preparation for intravenous injection, which comprises the steps of: fractionating an immunoglobulin-containing solution with 4 to 10 w/v% of polyethylene glycol having a molecular weight of from 1,000 to 10,000, at a pH value of from 4.5 to 6.5, an ionic strength of from 0.0001 to 0.1 M and a temperature of from 0 to 4° C. to recover a supernatant fraction; and concentrating the supernatant fraction at a pH of from 3.5 to 5.0.

Abstract: A chemo-physiological structure and method for forming the chemo-physiological structure. In a first embodiment, a cell of an animal is provided. The cell has a membrane surface and a viral receptor coupled to the membrane surface. A linker molecule having a covalently attached polymer is covalently bonded to the membrane surface, the viral receptor, or both. The polymer prevents an extracellular virus from bonding to the viral receptor. In a second embodiment, a linker molecule having a covalently attached polymer is covalently bonded to a capsid of a virus, which prevents the virus from bonding to a viral receptor of an adjacent or nearby animal cell.

Abstract: A drug which protects individuals against hepatitis C virus (HCV) is made of HCV hyperimmune globulins, which guarantee a substantial hyperimmunity against HCV thanks to a substantial hyperconcentration of virus C neutralizing antibodies. This hyperconcentration is obtained from blood of a large number of anti-HCV positive blood donors. The material used for the preparation of the HCV hyperimmune globulins is made of up to 100% of anti-HCV positive blood units.

Abstract: A method for the sterilization of a virus infected plasma or plasma derivative comprising contacting the plasma or plasma derivative with at least one organic solvents with or without at least one detergent and simultaneously or sequentially with a lipophilic adorbent at a temperature of 30° C. to 70° C.

Abstract: A process of preparing a double-sterilized immunoglobulin product for intravenous injection includes dissolving Cohn's component II in distilled ice water, and adjusting to the desired pH using acetic acid. A filter is used to remove alcohol and salt and establish a desired sodium ion concentration, and the immunoglobulin concentration is adjusted to form interim product, which is bottled. The bottle is filled with gaseous carbon dioxide to achieve a pressure of 0.7 to 200 kPa, sealed in the absence of any protectant, and sterilized. The interim product is filtered, concentrated to achieve an immunoglobulin concentration of 5% to 10%, adjusted to a desired pH, filtered to remove bacteria, and stored at room temperature for 21 days. Glucose is added in order to change the osmotic pressure equilibrium of said interim product to form final product.

Abstract: The present invention relates to a process for purifying immunoglobulin G from a crude immunoglobulin-containing plasma protein fraction. Said process includes a number of steps of which the anion exchange chromatography and the cation exchange chromatography are preferably connected in series. An acetate buffer having a pH of about 5.0-6.0 and having a molarity of about 5-25 mM is preferably used throughout the purification process. The invention further comprises an immunoglobulin product which is obtainable by this process. The invention also relates to an immunoglobulin product which has a purity of more than 98%, has a content of IgG monomers and dimers of more than 98.5%, has a content of IgA less than 4 mg of IgA/l, and contains less than 0.5% polymers and aggregates. Said product does not comprise detergent, PEG or albumin as a stabilizer. The product is stable, virus-safe, liquid and ready for instant intravenous administration.