Efficient mass production of purified recombinant porcine IL-2 with baculovirus/insect cell culture gene expression system

被引：0

作者：

Inumaru, S ^{[1
]}

Suegami, S ^{[1
]}

Kokuho, T ^{[1
]}

Yamamoto, M ^{[1
]}

Nishikawa, S ^{[1
]}

Watanabe, S ^{[1
]}

Kubota, T ^{[1
]}

机构：

[1] Natl Inst Anim Hlth, Tsukuba, Ibaraki 305, Japan

来源：

PROCEEDINGS OF THE INTERNATIONAL CYTOKINE SOCIETY ANNUAL MEETING | 2003年

关键词：

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

To develop an efficient mass production system of purified cytokines, we attempted to use a bioreactor and produced porcine interleukin-2 (poIL-2). The poIL-2 recombinant baculovirus infected insect cell line SF21AE was incubated in the bioreactor with 6 L of serum free medium for 72 hrs. This culture fluid contained 84 mg/L (purity: 65%) of recombinant poIL-2 (rpoIL-2). Three Litres of the fluid was filtered with 300kDa ultra-filter to remove virus particles etc. and concentrated by 10kDa ultra-filtration. The rpoIL-2 in the concentrate was precipitated between 65% and 90% saturation of ammonium sulfate. The precipitate was dissolved and dialyzed against PBS. Finally, 15.5 ml of the rpoIL-2 containing fraction (5.4 mg/ml, total: 84 mg, recovery: 33%) was prepared. Purity was 94.2%.

引用

页码：133 / 137

页数：5

共 50 条

[11] Time reduction and process optimization of the baculovirus expression system for more efficient recombinant protein production in insect cells
Philipps, B
Rotmann, D
Wicki, M
Mayr, LM
Forstner, M
PROTEIN EXPRESSION AND PURIFICATION, 2005, 42 (01) : 211 - 218
[12] Production and Purification of Recombinant Enteropeptidase Expressed in an Insect-Baculovirus Cell System
Azhar, Mahammad
Somashekhar, R.
PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY, 2015, 45 (03): : 268 - 278
[13] Factors affecting recombinant protein yields in insect cell baculovirus expression system
Tarui, H
Kawaguchi, H
Kaneko, S
Hara, T
JOURNAL OF THE FACULTY OF AGRICULTURE KYUSHU UNIVERSITY, 1995, 40 (1-2): : 45 - 51
[14] Expression of biologically active recombinant porcine GM-CSF by baculovirus gene expression system
Inumaru, S
Kokuho, T
Denham, S
Denyer, MS
Momotani, E
Kitamura, S
Corteyn, A
Brookes, S
Parkhouse, RME
Takamatsu, H
IMMUNOLOGY AND CELL BIOLOGY, 1998, 76 (03): : 195 - 201
[15] Protein Production Using the Baculovirus-Insect Cell Expression System
Contreras-Gomez, A.
Sanchez-Miron, A.
Garcia-Camacho, F.
Molina-Grima, E.
Chisti, Y.
BIOTECHNOLOGY PROGRESS, 2014, 30 (01) : 1 - 18
[16] Developing baculovirus-insect cell expression systems for humanized recombinant glycoprotein production
Jarvis, DL
VIROLOGY, 2003, 310 (01) : 1 - 7
[17] An efficient medium for high protein production in insect/baculovirus expression system.
Jesionowski, GA
Ataai, MM
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 1997, 213 : 152 - BIOT
[18] Simultaneous expression of recombinant proteins in the insect cell-baculovirus system: Production of virus-like particles
Palomares, Laura A.
Mena, Jimmy A.
Ramirez, Octavio T.
METHODS, 2012, 56 (03) : 389 - 395
[19] HIGH-LEVEL RECOMBINANT PROTEIN-PRODUCTION IN BIOREACTORS USING THE BACULOVIRUS INSECT CELL EXPRESSION SYSTEM
CARON, AW
ARCHAMBAULT, J
MASSIE, B
BIOTECHNOLOGY AND BIOENGINEERING, 1990, 36 (11) : 1133 - 1140
[20] Optimal production of recombinant protein by the baculovirus-insect cell system in shake-flask culture with medium replacement
Yamaji, H
Tagai, S
Fukuda, H
JOURNAL OF BIOSCIENCE AND BIOENGINEERING, 1999, 87 (05) : 636 - 641

← 1 2 3 4 5 →