Cargando…
Active protein aggregates induced by terminally attached self-assembling peptide ELK16 in Escherichia coli
BACKGROUND: In recent years, it has been gradually realized that bacterial inclusion bodies (IBs) could be biologically active. In particular, several proteins including green fluorescent protein, β-galactosidase, β-lactamase, alkaline phosphatase, D-amino acid oxidase, polyphosphate kinase 3, malto...
Autores principales: | Wu, Wei, Xing, Lei, Zhou, Bihong, Lin, Zhanglin |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3045283/ https://www.ncbi.nlm.nih.gov/pubmed/21320350 http://dx.doi.org/10.1186/1475-2859-10-9 |
Ejemplares similares
-
Recombinant production of medium- to large-sized peptides in Escherichia coli using a cleavable self-aggregating tag
por: Zhao, Qing, et al.
Publicado: (2016) -
Active tyrosine phenol-lyase aggregates induced by terminally attached functional peptides in Escherichia coli
por: Han, Hongmei, et al.
Publicado: (2020) -
Streamlined protein expression and purification using cleavable self-aggregating tags
por: Xing, Lei, et al.
Publicado: (2011) -
Small surfactant-like peptides can drive soluble proteins into active aggregates
por: Zhou, Bihong, et al.
Publicado: (2012) -
Formation of active inclusion bodies induced by hydrophobic self-assembling peptide GFIL8
por: Wang, Xu, et al.
Publicado: (2015)