Cj Cheiljedang Corporation

Cj Healthcare Corporation

Cheiljedang Corp.

Alteogen, Inc.

Dong Eok Lee

Jee Won Ahn

Ki Wan Kim

Min Ji Baek

Myung Suk Oh

Hyung Ki Park

Ji Hyun Moon

Ji Sook Park

Jong Sang Chung

Won Jeong Lee

Chung Min Lee

Hoo Keun Oh

Yoon Jung Lee

Sang Hyun Lee

Eun Young Choi

Soon Jae Park

Young Gi Kim

Yang Je Cho

Hyun Su Kim

Je Hak Kim

Young Joon Park

Sun Pyo Hong

Sang Mee Lee

Dal Hyun Kim

Hyoung Taek Lim

Chi Hye Park

Wang Don Yoo

Hye Shin Chung

Wan Je Park

Ree An Yoo

Nam Joong Lee

Kap Soo Noh

Suk Hoon Ha

Kyung Hwa Kim

Jung Min Yoo

Jung Rok Lee

Sung Yoo Cho

Chang Bong Jun

Gil Bu Kang

Gyong Sik Ha

Se Jun Kim

Yoo Hee Yang

The present invention relates to a method for purifying darbepoetin alfa by selectively separating only a structural isoform having a high content of sialic acid from a mixture of structural isoforms of darbepoetin alfa having various contents of sialic acid. Since the method of the present invention is a novel method for purifying darbepoetin alfa which can be conveniently and simply produced, it is possible to remarkably increase productivity due to process efficiency improvement, as well as to yield high purity darbepoetin alfa when mass-producing darbepoetin alfa according to the present invention.

Method for purifying darbepoetin alfa

The present invention relates to a long-acting human growth hormone NexP-hGH protein and its production method. More specifically, it relates to a specific isoform of long-acting human growth hormone NexP-hGH protein in which human growth hormone is fused with a highly glycosylated alpha-1 antitrypsin mutant whereby long-acting properties in vivo are increased. The present invention also relates to a high-purity purification method for NexP-hGH, which includes the steps of: (a) carrying out anion-exchange resin chromatography on a biological emulsion comprising NexP-hGH in which human growth hormone is fused with an alpha-1 antitrypsin mutant; (b) carrying out hydrophobic resin chromatography on the biological emulsion comprising NexP-hGH, or on the eluate produced in step (a); and (c) carrying out affinity chromatography, entailing packing with a resin to which anti-alpha-1 antitrypsin antibody fragments are attached, on the biological emulsion comprising NexP-hGH and on the eluate produced in step (a) or step (b).

Method of purifying a long-acting human growth hormone

Provided is a process for purifying human interferon beta from a recombinant human interferon beta-containing culture comprising performing affinity chromatography and cation exchange chromatography, wherein the affinity chromatography includes: adsorbing the interferon beta-containing culture to an equilibrated affinity chromatography column, followed by washing with an equilibration buffer solution; washing the column with a washing buffer solution A of pH 6.5-7.5 containing 30-60 wt % of propylene glycol and a washing buffer solution B of pH 6.5-7.5 containing 10-30 wt % of propylene glycol and 1-2M NaCl; and eluting a human interferon beta-containing fraction with a buffer solution of pH 6.5-7.5 containing 40-60 wt % of propylene glycol and 1-2M NaCl.

Process for purifying interferon beta

Provided is a process for purifying human interferon beta from a recombinant human interferon beta-containing culture comprising performing affinity chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC), wherein the affinity chromatography includes: adsorbing the interferon beta-containing culture to an equilibrated affinity chromatography column, followed by washing with an equilibration buffer solution; washing the column with a washing buffer solution A of pH 6.5-7.5 containing 30-60 wt % of propylene glycol and a washing buffer solution B of pH 6.5-7.5 containing 10-30 wt % of propylene glycol and 1-2M NaCl; and eluting a human interferon beta-containing fraction with a buffer solution of pH 6.5-7.5 containing 40-60 wt % of propylene glycol and 1-2M NaCl.

The present invention relates to a vaccine prepared from an attenuated Pseudomonas aeruginosa strains which are obtained by isolating Pseudomonas aeruginosa in a pure state according to the Fisher-Devlin immunotype and then repeatedly purifying the isolated strain, particularly CFCPA 10142 (KCCM 10029), CFCPA 20215 (KCCM 10030), CFCPA 30720 (KCCM 10031), CFCPA 40057 (KCCM 10032), CFCPA 50243 (KCCM 10033), CFCPA 60534 (KCCM 10034) and CFCPA 70018 (KCCM 10035) strains. In addition, the present invention relates to a process for preparing the vaccine for immunization against Pseudomonas aeruginosa infection which contains cell wall proteins having molecular weights ranging from 10,000 to 100,000. The cell wall protein component of the attenuated strain is non-pathogenic and safe, and exhibits excellent antibody formation capacity and is useful for preparation of a vaccine and therapeutic agent. The cell wall proteins exhibit an excellent cross-protective efficacy for various Pseudomonas aeruginosa strains and a superior antibody inducing property.

Process for preparing a vaccine against pseudomonas aeruginosa using

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Seoul, South Korea

Dong Eok Lee