Document Detail


Simple procedures for the construction of a robust and cost-effective cell-free protein synthesis system.
MedLine Citation:
PMID:  16797767     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In this study, as a part of our efforts to improve the robustness and economical feasibility of cell-free protein synthesis, we developed a simple method of preparing the cell extracts used for catalyzing cell-free protein synthesis reactions. We found that the high-speed centrifugation, pre-incubation, and dialysis steps of the conventional procedures could be omitted without losing the translational activity of the resulting cell extract. Instead, a simple centrifugation step at low speed (12,000 RCF for 10 min) followed by a brief period of incubation was sufficient for the preparation of an active extract to support cell-free protein synthesis with higher productivity and consistency. Compared to the present standard procedures for the preparation of the S30 extract, the overall cost of the reagents and processing time were reduced by 80 and 60%, respectively.
Authors:
Tae-Wan Kim; Jung-Won Keum; In-Seok Oh; Cha-Yong Choi; Chang-Gil Park; Dong-Myung Kim
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-05-27
Journal Detail:
Title:  Journal of biotechnology     Volume:  126     ISSN:  0168-1656     ISO Abbreviation:  J. Biotechnol.     Publication Date:  2006 Dec 
Date Detail:
Created Date:  2006-10-30     Completed Date:  2007-01-03     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8411927     Medline TA:  J Biotechnol     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  554-61     Citation Subset:  IM    
Affiliation:
School of Chemical and Biological Engineering, College of Engineering, Seoul National University, Seoul 151-742, Republic of Korea.
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MeSH Terms
Descriptor/Qualifier:
Cell-Free System
Chloramphenicol O-Acetyltransferase / biosynthesis,  genetics,  metabolism
Cost-Benefit Analysis*
Escherichia coli / chemistry,  genetics,  growth & development
Feasibility Studies
Protein Biosynthesis*
Protein Modification, Translational
Ribosomal Proteins / chemistry,  metabolism
Time Factors
Chemical
Reg. No./Substance:
0/Ribosomal Proteins; EC 2.3.1.28/Chloramphenicol O-Acetyltransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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