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Expression and purification of ubiquitin-specific protease (UBP1) of Saccharomyces cerevisiae in recombinant Escherichia coli
- Issue Date
- Nov-2005
- Publisher
- KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING
- Keywords
- ubiquitin-specific protease; UBP1; Saccharomyces cerevisiae; Escherichia coli
- Citation
- BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.10, no.6, pp.599 - 602
- Journal Title
- BIOTECHNOLOGY AND BIOPROCESS ENGINEERING
- Volume
- 10
- Number
- 6
- Start Page
- 599
- End Page
- 602
- ISSN
- 1226-8372
- Abstract
- Truncated form of UBP1, an ubiquitin-specific protease of Saccharomyces cerevisiae, was overexpressed in Escherichia coli. The hexahistidine residue (His(6)) was fused to the N-terminus of truncated UBP1 and the corresponding recombinant protein was purified with high yield by immobilized metal affinity chromatography. The truncated form of UBP1 protein was functional to cleave ubiquitinated human growth hormone as substrate. Effects of pH and temperature were investigated in order to optimize deubiquitinating reactions for the truncated UBP1. Optimum temperature and pH for the cleavage reaction were 40 degrees C and pH 8.0, respectively.
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Related Researcher
- Park, Kyung moon
- Science & Technology (Biological and Chemical Engineering)