Fisheries and Aquatic Sciences
- Volume 4 Issue 2
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- Pages.84-87
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- 2001
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- 2234-1757(eISSN)
The High Production of Multimeric Angiotensin-converting-enzyme-inhibitor in E. coli
- Park Je-Hyoen (Department of Biotechnology and Bioengineering, Pukyong National University) ;
- Kim Sun-Hoi (Department of Biotechnology and Bioengineering, Pukyong National University) ;
- Ahn Sun-Hee (Department of Biotechnology and Bioengineering, Pukyong National University) ;
- Lee Jong-Hee (Department of Biotechnology and Bioengineering, Pukyong National University) ;
- Kim Young-Sook (Department of Food Science and Technology, Yangsan College) ;
- Lee Sang-Jun (Biotechnology Division, National Fisheries Research & Development Institute) ;
- Kong In-Soo (Department of Biotechnology and Bioengineering, Pukyong National University)
- Published : 2001.06.01
Abstract
Multimeric angiotensin-converting-enzyme-inhibitor (ACE}) containing a trypsin cleavable linker peptide between ACEI was constructed. We made synthetic DNA coding for the ACEI peptide with asymmetric and complementary cohesive ends of linker nucleotides. A tandemly repeated DNA cassette for the expression of concatameric short peptide multimers was constructed by ligating the basic units. The resultant multimeric peptide expressed as soluble and trypsin treated peptide was shown at the same retention time with chemically synthetic ACEI by HPLC. The present results showed that the technique developed for the production of the ACEI multimers with trypsin cleavable linker peptides can be generally applicable to the production of short peptide.