Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1176810 | Analytical Biochemistry | 2006 | 6 Pages |
Abstract
A method for the rapid generation of intact proteins in a cell-free protein synthesis system was developed. The productivity of the recombinant proteins from the polymerase-chain-reaction-amplified templates was enhanced remarkably using an optimized translation enhancer sequence. The extra amino acid residues derived from the translation enhancer sequence were effectively removed by utilizing the appropriate detergent and peptide cleavage enzyme in the reaction mixture. These results demonstrate the versatility of cell-free protein synthesis in providing optimized and customized reaction conditions for the efficient production of the desired proteins.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Jeong-Mi Son, Jin-Ho Ahn, Mi-Yeon Hwang, Chang-Gil Park, Cha-Yong Choi, Dong-Myung Kim,