Title : Amino acid
sequence and post-translational modification of human
interleukin 2
Abstract :
- Human interleukin 2 was separated into multiple molecular forms by selective immunoaffinity chromatography and chromatofocusing
- For the most part, this heterogeneity was attributed to variations in glycosylation of the threonine residue in position 3 of the polypeptide chain
- The various molecular forms of interleukin 2 had nearly identical specific activities in the in vitro proliferation assay, indicating that the glycosylation had no significant effect on this response
- The entire primary sequence of interleukin 2 , including the location of the intramolecular disulfide bridge, was determined by a combination of peptide mapping and protein sequencing
- This information should aid in the determination of the active site(s) of the molecule