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 quality control material composition or a standard material for clinical laboratory tests, containing recombinant human serum albumin prepared by recombinant technology as a base component.

Abstract: A production method of a heterologous protein, comprising culturing a heterologous protein-producing host prepared by gene manipulation in a medium containing a fatty acid or a salt thereof, and a surfactant and harvesting the heterologous protein from the culture. The production amount of the heterologous protein produced by a heterologous protein-producing host can be increased. Moreover, since decomposition of the heterologous protein by an enzyme derived from the host can be inhibited, enabling large scale production of a heterologous protein.

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.degree. C. to recover a supernatant fraction; and concentrating the supernatant fraction at a pH of from 3.5 to 5.0.

Abstract: An immunoglobulin preparation comprising an immunoglobulin, wherein the preparation contains, as a contaminant, serum albumin in an amount not greater than 10 .mu.g per 50 mg of immunoglobulin; and/or wherein the preparation is free of fine particles which can serve as a nucleus of insoluble foreign matter, and processes for preparing the immunoglobulin preparation are described.

Abstract: A method for producing antithrombin-III from an antithrombin-III-containing aqueous solution, comprising at least one of the following steps (a) and (b): (a) heating the antithrombin-III-containing aqueous solution in the presence of a stabilizing agent so that 85% or more of the activity of antithrombin-III before the heating is maintained after the heating, and that the ratio of an antithrombin-III monomer after the heating is maintained at 95% or more; and (b) treating the antithrombin-III-containing aqueous solution with a metal chelate resin and recovering a purified antithrombin-III.

Abstract: A method for purifying human antithrombin III in an alcoholic solution at low temperature using bound heparin is provided.

Abstract: A method of preparing an IgA rich preparation comprising exposing a plasma fraction to an amino acid, organic salt or inorganic salt with optional chromatographic treatment yielding a product suitable for use in medical conditions treatable with IgA.

Abstract: The present invention describes a process for activating Factor II to Factor II.sub.a by incubating Factor II in the presence of Factor V, Factor X.sub.a, phospholipids, and calcium ions. Each of the factors is prepared from a single impure protein fraction which includes Factors II, V and X. The Factor II, V and X purification procedure comprises the steps of DEAE ligand chromatography and precipitation by the addition of barium chloride. Factor V is recovered from the barium chloride supernatant, and Factors II and X are contained in the barium chloride precipitate. The barium chloride precipitate is dissolved in an aqueous solution and is applied to a chromatographic resin coupled with a ligand which binds Factor X and Factor II weakly or not at all. Factor II is recovered from the fraction, which remains unbound or weakly bound to the Factor X binding ligand. Factor X.sub.

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 purifying human serum albumin which comprises subjecting human serum albumin-containing solution to heat treatment of about 50.degree.-70.degree. C. for 1-5 hours in the presence of acetyltryptophan and/or an organic carboxylic acid with 6-12 carbon atoms or a salt thereof.

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 monoclonal antibody is described, having a specific reactivity with a cancer-associated antigen selected from pancreas cancer-associated antigen, intestinum crassum cancer-associated antigen and hepatoma-associated antigen and has the following characteristics:(1) it exists in a blood serum of pancreas cancer, intestinum crassum cancer and hepatoma patients;(2) it comprises glycoproteins;(3) it has a molecular weight of about 700,000 to 1,500,000, as measured by gel-filtration and determined by comparison with that of a known protein;(4) it has a maximum absorption of 2800 nm when dissolved in 0.1 M acetic acid buffer solution (pH 4.5); and(5) it is released at least in a cultured supernatant medium of establihed cell line of COLO-201, TE-1, TE-2, TE-3, NRC-12, MKN-45 and KATO III. The monoclonal antibody is utilized as a reagent for detecting pancreas cancer, intestinum crassum cancer and hepatoma. A process for preparing the monoclonal antibody and a process for preparing the reagent are also disclosed.

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: Virus-contaminated immunoglobulin can be virus-inactivated by heating it in a substantially dry state at a temperature of 30.degree. to 100.degree. C. for a period of time sufficient for inactivating virus with maintaining original activity of the immunoglobulin. The addition of glycine, sodium chloride, sodium acetate, polyethylene glycol, albumin or mannitol enhances the effect and gives good solubility and good state to the solution of the virus-inactivated immunoglobulin.

Abstract: A process for the purification of HBsAg is disclosed, which comprises adsorbing specifically on a carrier, in the presence of an inorganic salt in an amount of 5 to 25 W/V %, an HBsAg obtained by gene engineering.

Abstract: A dry .gamma.-globulin preparation capable of intravenous injection which is obtainable by polyethylene glycol fractionation of plasma is improved in its water-solubility and stability against increase of anticomplement activity and decrease of antibody titer by purifying the .gamma.-globulin fraction with respect to protein to render the residual polyethylene glycol substantially not detectable in its 5% W/V solution, adding 0.2 to 2 parts by weight of glucose based on 1 part of .gamma.-globulin, and lyophilizing its solution.

Abstract: A live mumps vaccine can be stabilized to a great extent by adding in an amount, effective for stabilizing said vaccine, at least one stabilizer selected from the group consisting of albumin and gelatin.