Article
Isolation and refolding of a mutant methionine-free interleukin-2-receptor alpha chain synthesized as a fusion protein in Escherichia coli.
European journal of biochemistry - 1 Jul 1994
Seipelt I, Engels J W
Abstract excerpt
A soluble domain of the interleukin(IL)-2 receptor, the alpha chain synthesized in Escherichia coli, was employed to study expression and refolding of the protein. The results showed that it is possible to obtain biologically active synthetic methionine-free IL-2 receptor alpha chain (synIL-2R al...
Topics
- Amino Acid Sequence
- Base Sequence
- Cloning, Molecular
- DNA, Recombinant
- Escherichia coli
- Genes, Synthetic
- Humans
- Methionine
- Molecular Sequence Data
- Mutation
- Protein Folding
- Receptors, Interleukin-2
- Recombinant Fusion Proteins
- beta-Galactosidase