Related Experiment Video
Updated: Aug 13, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
Published on: May 22, 2018
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.
More Related Videos
Related Concept Videos
Protein Organization
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Proteins: From Genes to Degradation
Transcription is the synthesis of RNA molecules by RNA...
Leaky Scanning
Signal Sequences and Sorting Receptors
Bacterial Protein Maturation

