Ontology highlight
ABSTRACT:
SUBMITTER: Wojtowicz A
PROVIDER: S-EPMC1156937 | biostudies-other | 2005 May
REPOSITORIES: biostudies-other
Wojtowicz Anna A Mazurkiewicz-Pisarek Anna A Plucienniczak Grazyna G Mikiewicz-Sygula Diana D Chojnacka Luiza L Lukasiewicz Natalia N Plucienniczak Andrzej A
Microbial cell factories 20050530 1
BACKGROUND: It has been shown that proteins fused to ubiquitin undergo greater expression in E. coli and are easier to purify and renaturate than nonhybrid foreign proteins. However, there is no commercial source of large quantities of specific deubiquitinating proteases. This is the reason why hybrid proteins containing ubiquitin at their N-end cannot be used in large scale biotechnological processes. RESULTS AND CONCLUSION: We have described the synthesis of the yeast deubiquination enzyme UBP ...[more]