Stable activity of a deubiquitylating enzyme (Usp2-cc) in the presence of high concentrations of urea and its application to purify aggregation-prone peptides
- Research Center for Proteineous Materials (RCPM), Department of Bio-materials Engineering, Chosun University, Gwanju 501-759 (Korea, Republic of)
- Research Center for Proteineous Materials (RCPM), Department of Bio-materials Engineering, Chosun University, Gwanju 501-759 (Korea, Republic of) and Cell and Molecular Biology, College of Medicine, Chosun University, Gwanju 501-759 (Korea, Republic of)
Chemical synthesis of long or aggregation-prone peptide has been problematic. Its biological production has an advantage in that point, but it often forms inclusion body which creates difficulties in recovery of targets. As a deubiquitylating enzyme (Usp2-cc) was shown in this study to maintain its activity even in the presence of up to 4 M urea, target peptide was purified by a single step of chromatography after overexpression as inclusion body, solubilization in urea and cleavage by the enzyme from the fusion protein consisting of GroES (used for high expression and easy to handle), ubiquitin (as a cleavage site) and target peptide. This system is a convenient tool for production of peptides that are difficult to be chemically synthesized and biologically purified.
- OSTI ID:
- 20991478
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 359, Issue 3; Other Information: DOI: 10.1016/j.bbrc.2007.05.186; PII: S0006-291X(07)01182-5; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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