Abstract: A recombinant avian infectious coryza vaccine and a process for preparing the same are provided. A process for preparing a recombinant avian infectious coryza vaccine which comprises step of constructing E. coli that may produce as an inclusion body a fusion peptide consisting of peptides derived from outer-membrane protein of Avibacterium paragarinarum serotype A and serotype C, step of culturing said E. coli and collecting and purifying inclusion body from culture, and step of preparing a preparation comprising said purified inclusion body, and an avian infectious coryza vaccine comprising as an active ingredient the fusion peptide. A linker sequence may be inserted between the respective peptides comprising the fusion peptide. For the peptide derived from the serotypes A and C, an amino acid sequence region of Region 2 or its vicinity responsible for protection from infection may be used.

Abstract: A recombinant avian infectious coryza vaccine and a process for preparing the same are provided. A process for preparing a recombinant avian infectious coryza vaccine which comprises step of constructing E. coli that may produce as an inclusion body a fusion peptide consisting of peptides derived from outer-membrane protein of Avibacterium paragarinarum serotype A and serotype C, step of culturing said E. coli and colleting and purifying inclusion body from culture, and step of preparing a preparation comprising said purified inclusion body, and an avian infectious coryza vaccine comprising as an active ingredient the fusion peptide. A linker sequence may be inserted between the respective peptides comprising the fusion peptide. For the peptide derived from the serotypes A and C, an amino acid sequence region of Region 2 or its vicinity responsible for protection from infection may be used.

Abstract: A method of enhancing the efficacy of a monoclonal antibody preparation wherein antigens from patients are tested for their reactivity with the antibody. An amino acid sequence of an expressed protein is deuced from a nucleotide sequence determined by isolation and analysis of a target molecule gene in a biopsy from a patient. This is compared with the previously determined amino acid sequence recognized by the monoclonal antibody preparation in order to assess the fitness of patients for administration of the monoclonal antibody preparation.

Abstract: A recombinant avian infectious coryza vaccine and a process for preparing the same are provided. A process for preparing a recombinant avian infectious coryza vaccine which comprises step of constructing E. coli that may produce as an inclusion body a fusion peptide consisting of peptides derived from outer-membrane protein of Avibacterium paragarinarum serotype A and serotype C, step of culturing said E. coli and colleting and purifying inclusion body from culture, and step of preparing a preparation comprising said purified inclusion body, and an avian infectious coryza vaccine comprising as an active ingredient the fusion peptide. A linker sequence may be inserted between the respective peptides comprising the fusion peptide. For the peptide derived from the serotypes A and C, an amino acid sequence region of Region 2 or its vicinity responsible for protection from infection may be used.

Abstract: A method for purifying a modified major mite allergen obtained by the genetic recombination technique and a purified modified major mite allergen obtained by said method for purification are provided.

Abstract: The present invention herein discloses a method for purifying human serum albumin, which is characterized in that it comprises the steps of heat-treating a human serum albumin-containing solution including impurities originated from a host cell, in the presence of a divalent cation such as calcium ion, magnesium ion, nickel ion, cobalt ion, iron ion and zinc ion to thus selectively allow the impurities to undergo agglutination. The present invention also provides the highly purified human serum albumin prepared by the foregoing method.

Abstract: A method for purifying a modified major mite allergen obtained by the genetic recombination technique and a purified modified major mite allergen obtained by said method for purification are provided.

Abstract: A heterologous protein free from an inducer and a method for producing said protein are provided. A method for producing a heterologous protein which comprises the step of optionally culturing at low temperature recombinant E. coli cells expressing a heterologous protein under control of a promoter capable of inducing expression through temperature shift and then culturing at high temperature said recombinant E. coli cells in the absence of an inducer to thereby allow for expression of said heterologous protein, or the step of culturing at high temperature said recombinant E. coli cells to thereby simultaneously allow for both cell proliferation and expression of said heterologous protein, and the heterologous protein obtained by said method that is free from an inducer. Such heterologous protein may include a major mite allergen, a secretary macrophage toxin from Actinobacillus pleuropneumoniae and a surface protective antigen (SpaA) of Erysipelothrix rhusiopathiae.

Abstract: A method for enhancing efficacy of a monoclonal antibody preparation is provided wherein antigens from patients are tested for their reactivity with said antibody. In accordance with the method of the invention, an amino acid sequence of an expressed protein is deduced from a nucleotide sequence determined by isolation and analysis of a target molecule gene in biopsy from patients and is compared with the previously determined amino acid sequence recognized by said monoclonal antibody preparation to thereby assess fitness of patients for administration of said monoclonal antibody preparation.

Abstract: The present invention herein discloses a method for purifying human serum albumin, which is characterized in that it comprises the steps of heat-treating a human serum albumin-containing solution including impurities originated from a host cell, in the presence of a divalent cation such as calcium ion, magnesium ion, nickel ion, cobalt ion, iron ion and zinc ion to thus selectively allow the impurities to undergo agglutination. The present invention also provides the highly purified human serum albumin prepared by the foregoing method.

Abstract: Multimers of human serum albumin are removed from a solution of human serum albumin containing the multimers by bringing the human serum albumin solution into contact with an anion-exchanger equilibrated with a buffer containing a salt in a concentration ranging from 10 to 150 mM and having a pH value ranging from 5 to 9.5.

Abstract: A method for preparing human serum albumin comprises the step of heat-treating a human serum albumin solution containing contaminants at a pH value in the proximity to the isoelectric point of the contaminants.

Abstract: The present invention relates to a method for purifying a calcium ion-binding protein by cation exchange chromatography. The present invention provide a method for isolating and purifying a calcium ion-binding protein in a simple and efficient manner from a liquid sample containing a calcium ion-binding protein and contaminants without any pretreatment such as addition of a chelating agent. More specifically, the present invention relates to a method for purifying a calcium ion-binding protein which comprises contacting said protein with a cation exchange carrier in the presence of calcium ions to let the said protein be adsorbed to the carrier, and after washing, eluting said protein, and to a calcium ion-binding protein having substantially no contaminants obtained by the method of the present invention.

Abstract: The present invention relates to a method for purifying a calcium ion-binding protein by cation exchange chromatography. The present invention provide a method for isolating and purifying a calcium ion-binding protein in a simple and efficient manner from a liquid sample containing a calcium ion-binding protein and contaminants without any pretreatment such as addition of a chelating agent. More specifically, the present invention relates to a method for purifying a calcium ion-binding protein which comprises contacting said protein with a cation exchange carrier in the presence of calcium ions to let the said protein be adsorbed to the carrier, and after washing, eluting said protein, and to a calcium ion-binding protein having substantially no contaminants obtained by the method of the present invention.

Abstract: A method for converting a multimer of human serum albumin into monomers thereof comprises the step of treating the multimer with an alkaline solution. This method permits the efficient and quite simple conversion of human serum albumin multimers into monomers thereof at a low cost.

Abstract: A method for preparing human serum albumin comprises the step of heat-treating a human serum albumin solution containing contaminants at a pH value in the proximity to the isoelectric point of the contaminants.

Abstract: Multimers of human serum albumin are removed from a solution of human serum albumin containing the multimers by bringing the human serum albumin solution into contact with an anion-exchanger equilibrated with a buffer containing a salt in a concentration ranging from 10 to 150 mM and having a pH value ranging from 5 to 9.5.

Abstract: The present invention relates to a method for purifying a calcium ion-binding protein by cation exchange chromatography. The present invention provide a method for isolating and purifying a calcium ion-binding protein in a simple and efficient manner from a liquid sample containing a calcium ion-binding protein and contaminants without any pretreatment such as addition of a chelating agent. More specifically, the present invention relates to a method for purifying a calcium ion-binding protein which comprises contacting said protein with a cation exchange carrier in the presence of calcium ions to let the said protein be adsorbed to the carrier, and after washing, eluting said protein, and to a calcium ion-binding protein having substantially no contaminants obtained by the method of the present invention.

Abstract: The present invention provides a t-PA medicinal preparation obtained by remarkably improving the solubility and stability of t-PA or modified t-PA. Nicotinamide or a derivative thereof is incorporated into t-PA or modified t-PA-containing solvent system. If necessary, a citrate buffer solution is also used. The t-PA-containing medicinal composition is in the form of, for example, a freeze-dried preparation.