Purification and characterization of recombinant bovine growth hormone produced in Escherichia coli

被引：0
作者：
Jang Won Choi
Sung II Kim
Se Yong Lee
机构：
[1] Soon Chun Hyang University,Hyonam Kidney Laboratory
[2] Korea University,Graduate School of Biotechnology
来源：
Biotechnology Letters | 1998年 / 20卷
关键词：
Column Chromatography; Glutamic Acid; IPTG; Inclusion Body; Temperature Shift;
D O I：
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学科分类号：
摘要：
Using the pUBJ10 plasmid containing the modified bovine growth hormone (bGH) cDNA, large production has been attempted in E. coli BL21 strain. The bGH was highly expressed upto the level of 35% of total cell proteins by IPTG induction and temperature shift to 40°C. The recombinant bGH (rbGH) was isolated from inclusion bodies by solubilization in 10 M urea and followed by DEAE-TOYOPEARL 650C ion exchange and Sephadex G-100 column chromatography. The pUBJ10-derived bGH was eluted at 25.28 min similar to the standard bGH (at 25.18 min) by reverse-phase HPLC. The analysis of N-terminal amino acid showed that the mature bGH has glutamic acid as a first amino acid in agreement with DNA sequencing data. The biological activity was indirectly measured by radioreceptor assay and compared with a pituitary-derived bGH.
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页码：269 / 273
页数：4
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