Details

Autor(en) / Beteiligte

• Na, K.I. (Seoul National University, Seoul, Republic of Korea)
• Kim, M.D. (Seoul National University, Seoul, Republic of Korea)
• Min, W.K. (Seoul National University, Seoul, Republic of Korea)
• Kim, J.A. (Seoul National University, Seoul, Republic of Korea)
• Lee, W.J. (Korea Institute of Industrial Technology, Incheon, Republic of Korea)
• Kim, D.O. (Kyung Hee University, Yongin, Republic of Korea)
• Park, K.M. (Hongik University, Jochiwon, Republic of Korea)
• Seo, J.H. (Seoul National University, Seoul, Republic of Korea), E-mail: jhseo94@snu.ac.kr

Titel

Expression and Purification of Ubiquitin-Specific Protease (UBP1) of Saccharomyces cerevisiae in Recombinant Escherichia coli

Ist Teil von

• Biotechnology and bioprocess engineering, 2005-11, Vol.10 (6)

Erscheinungsjahr

2005

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• 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.