Article
Recombinant-derived interleukin-1 alpha stabilized against specific deamidation.
Protein engineering - 1 Jan 2000
Wingfield P T, Mattaliano R J, MacDonald H R, Craig S, Clore G M, Gronenborn A M, Schmeissner U
Abstract excerpt
Recombinant-derived human interleukin-1 alpha (IL-1 alpha), purified from Escherichia coli, was resolved by isoelectric focusing on polyacrylamide gels into two species of isoelectric points (pI) 5.45 and 5.20, which constituted approximately 75% and approximately 25% of the total IL-1 alpha protein respectively. The pI 5.45 and pI 5.20 species were separated by chromatofocusing and subjected to N-terminal...
Topics
- Amino Acids
- Electrophoresis, Polyacrylamide Gel
- Interleukin-1
- Isoelectric Focusing
- Magnetic Resonance Spectroscopy
- Mutation
- Protein Conformation
- Recombinant Proteins