Cj Cheiljedang Corporation

Lg Cns Co., Ltd.

Alteogen, Inc.

Cj Healthcare Corporation

Green Cross Holdings Corporation

Jee Won Ahn

Dong Eok Lee

Ki Wan Kim

Min Ji Baek

Myung Suk Oh

Jong Sang Chung

Hyung Ki Park

Ji Sook Park

Sang Hyun Lee

Min Jung Kim

Soon Jae Park

Sung Woo Park

Young Joon Park

Ji Hyun Moon

Hyoung Taek Lim

Sang Mee Lee

Chi Hye Park

Nam Kyu Kang

Jeong Hye Yoon

Yoon Jung Lee

Hye Shin Chung

Won Jeong Lee

Hoo Keun Oh

Soo-kwang Kim

Chung Min Lee

Jung-Ae Lim

Dong Kuk Park

Kwan Young Ko

Gil Bu Kang

Chang Bong Jun

Sung Yoo Cho

Seung-Ho Baek

Geun Hye Yeo

Soo-Kwang Kim

Disclosed is a method for preparing a composition comprising factor VIII (FVIII) and von Willebrand factor (vWF), wherein the content of the von Willebrand factor (vWF) can be controlled by mixing the factor VIII (FVIII) with the von Willebrand factor (vWF) at an appropriate ratio after separately purifying the factor VIII (FVIII) and the von Willebrand factor (vWF) from plasma in a single process. The method can prepare and purify a composition comprising factor VIII (FVIII) and a varying content of von Willebrand factor (vWF) without increasing the amount of impurities other than the von Willebrand factor (vWF) compared to a method of purifying factor VIII (FVIII) separately, without significantly increasing the processing time (within 3 hours) compared to a method of purifying factor VIII (FVIII), and without changing the yield of factor VIII (FVIII).

Method of preparing composition containing factor VIII (FVIII) and von Willebrand factor (vWF) with controlled content of von Willebrand factor (vWF)

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

A method may provide an agent service to a user terminal by including receiving a user instruction from the user terminal, determining whether at least one agent reply to at least one keyword included in the user instruction is able to be searched for in a database, providing at least one suggestive query to the user terminal to allow a search for the at least one agent reply, receiving at least one set of additional information with respect to the at least one suggestive query from the user terminal, and providing the at least one agent reply to the user terminal based on the at least one set of additional information.

System and method for providing agent service to user terminal

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.

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Seoul, South Korea

Jee Won Ahn