한국생물공학회:학술대회논문집
- 2003.04a
- /
- Pages.554-556
- /
- 2003
Expression, purification and characterization of ubiquitin-specific pretense 1 for hydrolysis of ubiquitin-fused human growth hormone expressed in recombinant Escherichia coli
Abstract
This research was focused on expression, purification and characterization of ubiquitin-specific protease 1 (UBP1) expressed in recombinant Escherichia coli. Various systems were constructed by fusing polycationic fusion tails or fusion partners to the C- or N-terminus of the product protein. In particular, UBP1 containing 6 histidine residues at the N-terminal end showed best results in terms of expression level and purification efficiency. The N-terminal
본 연구에서는 고부가가치 의약단백질인 human growth hormone을 고순도로 얻기 위하여 재조합 대장균을 이용하여 ubiquitin이 융합된 형태로 단백질을 발현시키고, 이를 분해하는 ubiquitin-specific pretense를 발현시켜 이를 분리
Keywords