Abstract: Disclosed is a method for producing a fusion protein in which an antibody and a lysosomal enzyme are fused. The method is a method for producing a fusion protein in which an antibody and a human lysosomal enzyme are fused, the method including: (a) culturing mammalian cells producing the fusion protein in a serum-free medium to secrete the fusion protein in a culture medium; (b) collecting a culture supernatant by removing the mammalian cells from the culture medium; and (c) purifying the fusion protein from the culture supernatant by using a column chromatography using a material to which a substance having affinity for the antibody is bound as a solid phase, an anion exchange column chromatography, a cation exchange column chromatography, and a size exclusion column chromatography.

Abstract: Disclosed is a method for producing a fusion protein of human serum albumin and human growth hormone. The method comprises (a) a step of culturing a mammalian cell capable of producing the protein in a serum-free medium and causing the protein to be secreted into the culture fluid, (b) a step of collecting a culture supernatant by removing the mammalian cell from the culture fluid, and (c) a step of purifying the protein from the culture supernatant by using column chromatography using a material to which an antibody having an affinity for the protein is bound as a stationary phase, column chromatography using a material having an affinity for phosphate group as a stationary phase, cation exchange column chromatography, and size exclusion column chromatography.

Abstract: Disclosed is a method for production of a fusion protein in which an antibody and a lysosomal enzyme are fused. The method comprises; (a) a step of culturing mammalian cells producing the fusion protein in a serum-free medium to let the mammalian cells secrete the fusion protein in the culture medium, (b) a step of collecting culture supernatant by removing the mammalian cells from the culture medium, and (c) a step of purifying the fusion protein from the culture supernatant by using a column chromatography employing as a solid phase a material to which a substance having affinity for the fusion protein has been bound, a column chromatography employing as a solid phase a material having affinity for the phosphate group, and a size exclusion column chromatography.

Abstract: A distributed processing apparatus 1 includes: a selection unit 12 that lists execution plans for a query related to a plurality of database apparatuses 2 and selects any of the execution plans based on data transfer time periods of the individual execution plans; a transmission unit 13 that divides the query in accordance with the selected execution plan, and transmits instructions that include divided queries obtained by dividing the query and transfer destinations of execution results of the divided queries to the corresponding database apparatuses 2; and an output unit 14 that receives the execution result of the query from the database apparatus 2, and outputs the execution result.

Abstract: Disclosed is a highly efficient method for production of highly pure mutant-type human erythropoietin. The method is for production of mutant-type human erythropoietin, in which a transformed mammalian cell is allowed to produce the mutant-type human erythropoietin, and the supernatant of the culture is subjected to hydrophobic column chromatography, multimodal anion exchange column chromatography, anion exchange column chromatography, phosphate group affinity column chromatography, and gel filtration column chromatography, in this order.

Abstract: Provided are a novel medium for expressing glycoproteins by culturing cells and a method for producing glycoproteins by culturing cells in the medium. Further provided are a medium comprising uridine and N-acetyl-D-mannosamine for the use of expression of a glycoprotein by culturing cells and a method for producing glycoproteins by culturing cells in for medium.

Abstract: Provided are a novel medium for expressing glycoproteins by culturing cells and a method for producing glycoproteins by culturing cells in said medium. Further provided are a medium comprising uridine and N-acetyl-D-mannosamine for the use of expression of a glycoprotein by culturing cells and a method for producing glycoproteins by culturing cells in said medium.

Abstract: Disclosed is a method for production of a fusion protein in which an antibody and a lysosomal enzyme are fused. The method comprises; (a) a step of culturing mammalian cells producing the fusion protein in a serum-free medium to let the mammalian cells secrete the fusion protein in the culture medium, (b) a step of collecting culture supernatant by removing the mammalian cells from the culture medium, and (c) a step of purifying the fusion protein from the culture supernatant by using a column chromatography employing as a solid phase a material to which a substance having affinity for the fusion protein has been bound, a column chromatography employing as a solid phase a material having affinity for the phosphate group, and a size exclusion column chromatography.

Abstract: Provided are a novel medium for expressing glycoproteins by culturing cells and a method for producing glycoproteins by culturing cells in the medium. Further provided are a medium comprising uridine and N-acetyl-D-mannosamine for the use of expression of a glycoprotein by culturing cells and a method for producing glycoproteins by culturing cells in the medium.

Abstract: Disclosed is a highly efficient method for production of highly pure mutant-type human erythropoietin. The method is for production of mutant-type human erythropoietin, in which a transformed mammalian cell is allowed to produce the mutant-type human erythropoietin, and the supernatant of the culture is subjected to hydrophobic column chromatography, multimodal anion exchange column chromatography, anion exchange column chromatography, phosphate group affinity column chromatography, and gel filtration column chromatography, in this order.

Abstract: Disclosed are a novel expression vector for efficient expression of recombinant proteins in mammalian cells, a mammalian cell transformed with the vector, and a method for production of the mammalian cell. The expression vector is an expression vector for expression of a mammalian protein and includes a gene expression regulatory site, and a gene encoding the protein downstream thereof, and an internal ribosome entry site further downstream thereof, and a gene encoding a glutamine synthetase further downstream thereof, and a dihydrofolate reductase gene downstream of either the same gene expression regulatory site or another gene expression regulatory site in addition to the former.

Abstract: Provided are a novel medium for expressing glycoproteins by culturing cells and a method for producing glycoproteins by culturing cells in said medium. Further provided are a medium comprising uridine and N-acethyl-D-mannosamine for the use of expression of a glycoprotein by culturing cells and a method for producing glycoproteins by culturing cells in said medium.

Abstract: Disclosed are a novel expression vector for efficient expression of recombinant proteins in mammalian cells, a mammalian cell transformed with the vector, and a method for production of the mammalian cell. The expression vector is an expression vector for expression of a mammalian protein and includes a gene expression regulatory site, and a gene encoding the protein downstream thereof, and an internal ribosome entry site further downstream thereof, and a gene encoding a glutamine synthetase further downstream thereof, and a dihydrofolate reductase gene downstream of either the same gene expression regulatory site or another gene expression regulatory site in addition to the former.

Abstract: To provide a new technique by which efficient transfection is ensured in delivering a target gene into a cell, disclosed is a nucleic acid construct for nuclear import, which comprises a ternary complex consisting of a nucleic acid substance containing a gene to be delivered into the nucleus of a cell, an importin protein (for example, importin-?) capable of passing through the nuclear pore and involved in the nuclear transport, and a binding substance (for example, polyethyleneimine) bound to both of the nucleic acid substance and the importin protein. Nucleic acid transport from outside of a cell into the cell nucleus can be particularly promoted by administering the nucleic acid construct bound to a cell membrane receptor binding factor and/or a membrane fusing substance, or administering the nucleic acid construct encapsulated in a non-viral vector (for example, Sendai virus envelope) having cell membrane permeability and membrane fusing properties.

Abstract: To provide a new technique by which efficient transfection is ensured in delivering a target gene into a cell, disclosed is a nucleic acid construct for nuclear import, which comprises a ternary complex consisting of a nucleic acid substance containing a gene to be delivered into the nucleus of a cell, an importin protein (for example, importin-?) capable of passing through the nuclear pore and involved in the nuclear transport, and a binding substance (for example, polyethyleneimine) bound to both of the nucleic acid substance and the importin protein. Nucleic acid transport from outside of a cell into the cell nucleus can be particularly promoted by administering the nucleic acid construct bound to a cell membrane receptor binding factor and/or a membrane fusing substance, or administering the nucleic acid construct encapsulated in a non-viral vector (for example, Sendai virus envelope) having cell membrane permeability and membrane fusing properties.

Abstract: Single crystals of tetrabromobisphenol A having an average particle size of from 150 to 500 .mu.m, each having a polyhedral shape.