Abstract: A process for producing an intravenously-administrable gamma globulin solution substantially free of contaminating viruses by fractionating an impure gamma globulin solution and then treating the purified gamma globulin, in any order, with a solvent-detergent for viral inactivation and a heat treating for viral inactivation. Thereafter, denatured impurities, residual solvent and aggregate generated by the heat treatment are removed from the gamma globulin.

Abstract: A process for producing an intravenously-administrable gamma globulin solution substantially free of contaminating viruses by fractionating an impure gamma globulin solution and then treating the purified gamma globulin, with a solvent-detergent for viral inactivation and a heat treating for viral inactivation. Thereafter, denatured impurities, residual solvent and aggregate generated by the heat treatment are removed from the gamma globulin.

Abstract: A process for producing an intravenously-administrable gamma globulin solution substantially free of contaminating viruses by fractionating an impure gamma globulin solution and then treating the purified gamma globulin, in any order, with a solvent-detergent for viral inactivation and a heat treating for viral inactivation. Thereafter, denatured impurities, residual solvent and aggregate generated by the heat treatment are removed from the gamma globulin.

Abstract: A process for producing an intravenously-administrable gamma globulin solution substantially free of contaminating viruses by heat treating for viral inactivation and fractionating an impure gamma globulin solution and then treating the purified gamma globulin with a solvent-detergent for further viral inactivation. In a continuous process disclosed herein, partially purified gamma globulin solids is not recovered as an intermediate product during the disclosed process. In the continuous process, the fractionation to obtain a purified gamma globulin solution is carried out without precipitation of the desired gamma globulin.

Abstract: The present invention is directed to a process for purifying alpha-1-PI. The process comprises providing an impure protein fraction which comprises alpha-1-PI. The impure protein fraction is suspended in an aqueous solution at pH 6. Insoluble proteins are recovered and resuspended in aqueous solution at pH 8.5. PEG is added to precipitate .alpha.-2 proteins. To the PEG supernatant precipitation, which comprises alpha-1-PI, is added ZnCl.sub.2 to precipitate crude alpha-1-PI. The crude alpha-1-PI is resolubilized and applied to an anion-exchange medium. A fraction comprising alpha-1-PI is recovered from the anion-exchange medium. Alpha-1-PI purified by the process has a specific activity about 1.0 units/OD.sub.280.

Abstract: The present invention is directed to a process for purifying alpha-1-PI. The process comprises providing an impure protein fraction which comprises alpha-1-PI. The impure protein fraction is suspended in an aqueous solution at pH 6. Insoluble proteins are recovered and resuspended in aqueous solution at pH 8.5. PEG is added to precipitate .alpha.-2 proteins. To the PEG supernatant precipitation, which comprises alpha-1-PI, is added ZnCl.sub.2 to precipitate crude alpha-1-PI. The crude alpha-1-PI is resolubilized and applied to an anion-exchange medium. A fraction comprising alpha-1-PI is recovered from the anion-exchange medium. Alpha-1-PI purified by the process has a specific activity about 1.0 units/OD.sub.280.

Abstract: A liquid preparation of antithrombin-III (AT-III), comprising an AT-III and an organic acid, a salt thereof, a sugar sulfate or a surfactant as a stabilizer, and a liquid preparation of AT-III, having a pH of 9-10. The preparation of the present invention is stable after long-term preservation and poses no clinical problems in terms of pharmacological effects and safety. The preparation is more advantageous than lyophilized preparations in that it does not require dissolution in injectable distilled water and can be used easily. Accordingly, the preparation is clinically very useful.

Abstract: An albumin preparation having a polymer content of not more than 3% by weight based on the serum albumin content and an .alpha..sub.1 -AGP content of not more than a detectable limit based on the serum albumin content, which is prepared by removing a polymer-forming factor from an albumin aqueous solution by, for example, ion exchange separation or affinity chromatography, and subjecting the solution to a heat treatment.

Abstract: A method of producing a virus-inactivated protein-containing composition from a protein-containing composition which may be contaminated with virus. The method according to the present invention permits production of pharmaceutically safer virus-inactivated protein preparations without spoiling the protein activity.

Abstract: A method of fractionating plasma protein which comprises treating a plasma protein-containing material in the following sequence of steps, provided that steps (ii) through (v) may be performed in an optional order: (i) freeze-thaw treatment, (ii) treatment at 5 to 10% ethanol concentration, (iii) treatment with an anion exchanger, (iv) affinity chromatography with immobilized lysine, (v) affinity chromatography with immobilized heparin, (vi) treatment at 18 to 30% ethanol concentration, (vii) treatment at 35 to 45% ethanol concentration.

Abstract: A method of producing immunoglobulin preparations for intravenous injection which starts with an immunoblobulin-containing fraction and comprises the treatment steps of:(a) treating said fraction with 4-10 weight/volume percent of polyethylene glycol having a molecular weight of 1,000-10,000 under conditions of pH 4-6, ion strength 0.0001-0.1M and temperature 0.degree.-4.degree. C. and recovering the supernatant,(b) treating the supernatant obtained in step (a) with 10-15 weight/volume percent of polyethylene glycol having a molecular weight of 1,000-10,000 under conditions of pH 6-9, ion strength 0.0001-0.1M and temperature 0.degree.-4.degree. C. and recovering the resulting precipitate, and(c) heat-treating, in any desired step, said immunoglobulin in the presence of a stabilizer under conditions sufficient to inactivate contaminant viruses.

Abstract: A stable aqueous thrombin solution containing thrombin and a sugar and an amino acid as a stabilizer is disclosed. According to the present invention, there is provided a stable aqueous thrombin solution.

Abstract: An intravenously injectable solution of chemically unmodified .gamma.-globulin having a complete molecular structure is disclosed, said solution containing sorbitol as a stabilizer and having a low electrical conductivity and a pH of about 5.5.+-.0.2. The injectable solution does not cause an increase of .gamma.-globulin polymer, a rise of anticomplement titer, or impairment of the activities of the .gamma.-globulin, either during preservation or upon administration to a living body.

Abstract: A process for heat treating an aqueous solution containing chemically unmodified .gamma.-globulin, wherein said heat treating is carried out in the presence of sorbitol is disclosed. By the heat treatment, impurity viruses can be inactivated without causing impairment of activities of chemically unmodified .gamma.-globulin, increasing polymer contents or increasing an anticomplement titer.

Abstract: A fibronectin preparation in the form of an aqueous solution at least upon use is disclosed. The preparation contains at least one member selected from the group consisting of disaccharides, albumin and nonionic surface active agents as a stabilizer. The preparation has improved water-solubility when in use and high stability in an aqueous solution.

Abstract: It has been discovered that lysozyme in the blood is concentrated into the albumin fraction when the blood is fractionated by the alcohol fractionation method at lowered temperature or the ammonium sulfate fractionation method. Lysozyme can be produced by contacting the albumin fraction with a weakly acidic cation-exchanger such as CM-cellulose to adsorb selectively the lysozyme with the cation-exchanger and then eluting the lysozyme adsorbed from the cation-exchanger.

Abstract: A heat-stable plasma protein solution showing no blood pressure-depressing action is obtained by adding distilled water to a paste IV-1, a waste fraction obtained from the Cohn's cold ethanol plasma fractionation method and has heretofore been discarded as a waste, to extract water-soluble proteins in the paste, heat-treating the extract at pH 4.5 to 5.5 at 50.degree. to 65.degree. C. in the presence of an organic acid to remove as precipitates lipo- and glyco-proteins contained in the extract, adding Rivanol to the resulting supernatant to remove by precipitation residual lipo-proteins giving turbidity to the supernatant, and then removing blood pressure-depressing substances present in the resulting supernatant by adsorption with an inorganic adsorbent or cation exchanger. The thus obtained heat-stable plasma protein solution shows prominent effects in the therapy of shock by acute bleeding, burns, supply of protein nutrients, hypoproteinemia, etc., and is useful for medical treatments.