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: Disclosed is a method for production of recombinant human DNase I which is of such high purity as may be directly used as a medical drug. The method includes the steps of; culturing recombinant DNase I-producing mammalian cells, subjecting a culture supernatant to an anion-exchange column chromatography, subjecting to a column chromatography employing as solid phase a material having affinity for phosphate group, subjecting to a cation-exchange column chromatography, and subjecting to a dye affinity column chromatography.

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 is a method for production of recombinant human DNase I which is of such high purity as may be directly used as a medical drug. The method includes the steps of; culturing recombinant DNase I-producing mammalian cells, subjecting a culture supernatant to an anion-exchange column chromatography, subjecting to a column chromatography employing as solid phase a material having affinity for phosphate group, subjecting to a cation-exchange column chromatography, and subjecting to a dye affinity column chromatography.

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.