Article
Site-directed pegylation of recombinant interleukin-2 at its glycosylation site.
Bio/technology (Nature Publishing Company) - 1 Apr 1990
Goodson R J, Katre N V
Abstract excerpt
We have modified recombinant interleukin-2 (rIL-2) to facilitate site-directed covalent attachment of monomethoxy polyethylene glycol (PEG). The site chosen for modification and subsequent covalent attachment with PEG (PEGylation) was the single glycosylation position found in the native interleukin-2 (IL-2). The mutant protein was expressed in E. coli, purified, and PEGylated with a PEG-maleimide reagent to...
Topics
- Amino Acid Sequence
- Base Sequence
- Binding Sites
- Cloning, Molecular
- Cysteine
- Escherichia coli
- Glycosylation
- Interleukin-2
- Molecular Sequence Data
- Mutation
- Polyethylene Glycols