Downstream processes for recombinant human DNaseⅠfrom two different expression patterns in Escherichia coli

GUO XiongJun;CHEN JinChun

Journal of Beijing University of Chemical Technology ›› 2010, Vol. 37 ›› Issue (1) : 102-105.

PDF(1100 KB)
Welcome to Journal of Beijing University of Chemical Technology, Today is July 20, 2025
Email Alert  RSS
PDF(1100 KB)
Journal of Beijing University of Chemical Technology ›› 2010, Vol. 37 ›› Issue (1) : 102-105.
生物技术与环境工程

Downstream processes for recombinant human DNaseⅠfrom two different expression patterns in Escherichia coli

  • GUO XiongJun;CHEN JinChun
Author information +
History +

Abstract

The relationship between the induction temperature and the soluble expression of human DNase I in E. coli has been studied. It was found that human DNase Ⅰ protein assembled in inclusion bodies under 37℃ induction, whereas under 20℃ induction human DNaseⅠwas mostly (about 62.3%) secreted to the periplasmic space and showed DNase enzyme activity. The two kinds of human DNase Ⅰ protein from the two different expression patterns were purified. The results indicated that the enzyme activity of recombinant human DNase I from inclusion bodies was 592.2U/mg, and its recovery rate was 32.1%, whereas the activity of that from the periplasmic space was 1283U/mg, and the recovery rate was 24.1%. Furthermore, the purification process for DNaseⅠsecreted to the periplasmic space was easier than that for DNaseⅠassembled in inclusion bodies.

Cite this article

Download Citations
GUO XiongJun;CHEN JinChun. Downstream processes for recombinant human DNaseⅠfrom two different expression patterns in Escherichia coli[J]. Journal of Beijing University of Chemical Technology, 2010, 37(1): 102-105

References

[1]Kishi K, Yasuda T, Takeshita H. DNase I: Structure, function, and use
in medicine and forensic science[J]. Legal Medicine, 2001, 3(2): 69-83.
[2]张晴妮,徐骥, 李飞, 等. 重组小纤溶酶的制备及其生物学活性[J]. 中国生物制品学杂志, 2008, 21(8): 701-704.Zhang Q N, Xu J, Li F, et al. Preparation an
d biological activity of recombinant miniplasmin[J]. Chinese Journal of Bio
logicals, 2008, 21(8): 701-704. (in Chinese)
[3]孙传秀, 赵文志, 何盛为, 等. 重组人骨形态发生蛋白2在大肠杆菌中的可溶性表达和纯[J]. 中国组织工程研究与临床康复, 2009, 13(7): 1267-1270.Sun C X, Zhao W Z, He S W, et al. Soluble expression and purification of recombinant human bone morphogenetic protein2 gene in E. coli[J]. Journal of Clinical Rehabilitative Tissue Engineering Research, 2009, 13(7): 1267-1270. (in Chinese)
[4]Liu F J, Liao L, Chen J C. Preparation of unglycosylated human caseinomacropeptide by engineering DAB Escherichia coli[J]. Journal of Agricultural and Food Chemist
ry, 2008, 56(3): 889-893.
[5]Lai Q G, Liu S T, Lu W H, et al. Expression in Escherichia coli, purification and enzymatic properties of chicken aminopeptidase H[J]. Chinese Journal of Biotechnology, 2008, 24(3): 381-386.
[6]Nadane D, Yasuda T, Kishi K. Measurement of deoxyribonuclease Ⅰactivity i
n human tissues and body fluids by single radial enzymediffusion method[J].
Clinical Chemistry, 1993, 39(3): 448-452.
[7]Fujihara J, Takatsuka H, Kataoka K, et al. Two deoxyribonuclease I gene polymorphisms and correlation between genotype and its activity in Japanese population[J]. Legal Medicine, 2007, 9(5):233-236.
PDF(1100 KB)

3470

Accesses

0

Citation

Detail

Sections
Recommended

/