Jcr Pharmaceuticals Co., Ltd.

Atsushi Sugimura

Kazutoshi Mihara

Atsuko Kawasaki

Tsuyoshi Fukui

Yukichi Hatano

Yae Ito

Katsuya Daimon

Kenichi Takahashi

Hiroyuki Sonoda

Miroslav Matev

Shinji Kakimoto

Masahiro Asano

Shoichiro Kamei

Junya Tani

Toshihiro Yagi

Kouta Ootsuki

Yuukichi Hatano

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.

Method for production of mutant-type human erythropoietin

Disclosed is a method for production of recombinant human alpha-galactosidase A (rh alpha-Gal A) in a large scale, with a high purity. The method comprises the steps of (a) culturing rh alpha-Gal A-producing mammalian cells in a serum-free medium, (b) collecting culture supernatant, (c) subjecting the culture supernatant to anion-exchange column chromatography, (d) to hydrophobic column chromatography, (e) to a column chromatography employing as solid phase a material having affinity for phosphate group, (f) to cation-exchange column chromatography, (g) to dye-affinity column chromatography, and (h) to gel filtration column chromatography, in the order.

Method for production of recombinant human alpha-galactosidase A from material containing contaminant host cell proteins by chromatography

Disclosed is a method for production of recombinant human alpha-galactosidase A (rh alpha-Gal A) in a large scale, with a high purity. The method comprises the steps of (a) culturing rh alpha-Gal A-producing mammalian cells in a serum-free medium, (b) collecting culture supernatant, (c) subjecting the culture supernatant to anion-exchange column chromatography, (d) to hydrophobic column chromatography, (e) to a column chromatography employing as solid phase a material having affinity for phosphate group, (f) to cation-exchange column chromatography, and (g) to gel filtration column chromatography, in the order.

Method for production of recombinant human alpha-galactosidase A

Disclosed is a method for production of recombinant human iduronate 2-sulfatase (rhI2S) (the 26th to 550th amino acids of SEQ ID NO: 10) in a large scale, with a high purity, and mannose 6-phosphate residues. The method comprises the steps of (a) culturing rhI2S (the 26th to 550th amino acids of SEQ ID NO: 10)-producing mammalian cells in a serum-free medium, (b) collecting culture supernatant, (c) subjecting the culture supernatant to cation-exchange column chromatography, (d) to dye affinity column chromatography, (e) to anion-exchange column chromatography, and (f) to a column chromatography employing as solid phase a material having affinity for phosphate group, and (g) to gel filtration column chromatography, in the order.

Method for production of recombinant human iduronate 2-sulfatase

Disclosed is an efficient method for production of aminopeptidase. The method comprises either transforming host bacteria with an aminopeptidase gene and with a neutral protease gene, or transforming some part of host bacteria with an aminopeptidase gene while transforming the other part of the host bacteria with a neutral protease gene, culturing in a medium the hose bacteria transformed with the aminopeptidase gene and with the neutral protease gene, or culturing a mixture of the host bacteria transformed with the aminopeptidase gene and the host bacteria transformed with the neutral protease gene, to let both the aminopeptidase and the neutral protease be expressed, and collecting the aminopeptidase thus produced from the culture mixture.

Method for producing aminopeptidase

Disclosed is a method for production of recombinant human FSH in high yield and a high purity. The method comprises the steps of: (a) culturing recombinant human FSH-producing mammalian cells in a serum-free medium, (b) collecting culture supernatant, (c) subjecting the culture supernatant to cation-exchange column chromatography, (d) dye affinity column chromatography, (e) hydrophobic column chromatography, and (f) gel filtration column chromatography to collect recombinant human FSH-active fractions, in the order.

Method for production of recombinant human FSH

Growing community of inventors

Hyogo, Japan

Atsushi Sugimura