Article
Escherichia coli expression and processing of human interleukin-1 beta fused to signal peptides.
DNA and cell biology - 1 Apr 1990
Curry K A, Yem A W, Deibel M R, Hatzenbuhler N T, Hoogerheide J G, Tomich C S
Abstract excerpt
Escherichia coli expression, processing, and secretion of human interleukin-1 beta (IL-1 beta) fused to the signal peptide of E. coli OmpA or PhoA protein were studied. With fusion to either signal sequence, high-level expression was observed and the products accumulated to about 20% of total cell protein. In the fusion to OmpA leader sequence, more than 50% of the product has the OmpA signal peptide removed...
Topics
- Amino Acid Sequence
- Bacterial Outer Membrane Proteins
- Base Sequence
- Escherichia coli
- Humans
- Interleukin-1
- Molecular Sequence Data
- Mutation
- Osmotic Pressure
- Protein Engineering
- Protein Processing, Post-Translational
