scholarly journals High–level expression of housefly cecropin A in Escherichia coli using a fusion protein

2010 ◽  
Vol 3 (6) ◽  
pp. 421-426
Author(s):  
Xueli Zheng ◽  
Wei Wang
2000 ◽  
Vol 31 (2) ◽  
pp. 91 ◽  
Author(s):  
Adriana V. Ribas ◽  
Paulo L. Ho ◽  
Martha M. Tanizaki ◽  
Isaias Raw ◽  
Ana L.T.O. Nascimento

2014 ◽  
Vol 926-930 ◽  
pp. 997-1000
Author(s):  
Tong Yi Sun

The Cathelicidin OH-CATH30 may have therapeutic potential against the systemic infections. However, it is a great challenge to obtain abundant OH-CATH30 by Escherichia coli expression system. The OH-CATH30 coding sequence was optimized and subcloned into vector pET-32a, allowing the peptide to be expressed as a thioredoxin fusion protein. The highest protein expression level obtained was 100 mg/L of bacterial culture. Before being cleaved with enterokinase, the released recombinant OH-CATH30 exhibited a in vitro strong antibacterial activity against the control strains.


1996 ◽  
Vol 18 (2) ◽  
pp. 163-168 ◽  
Author(s):  
Kwang-Rae Huh ◽  
Eun Hee Cho ◽  
Soo Ok Lee ◽  
Doe Sun Na

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