title: Interleukin-2 self-association.
abstract: The self-association of human recombinant interleukin-2 (IL-2) from E. coli was explored. Self-association, with an apparent Kd of 0.6 micromolar, has pronounced effects on (1) the surface exposure of Trp-121, deduced from quenching studies employing potassium iodide and acrylamide, (2) the apparent quantum yield of Trp-121, the fluorescence of Trp-121 in IL-2 aggregates is 4-fold lower than in IL-2 "monomers", and (3) IL-2-mediated phospholipid vesicle fusion/aggregation.
authors.affiliation: Surgery Department, Case Western Reserve University School of Medicine, Ohio 44109.
authors.forename: J D
authors.initials: JD
authors.lastname: Fleischmann
authors.forename: D
authors.initials: D
authors.lastname: Wentworth
authors.forename: F
authors.initials: F
authors.lastname: Valencic
authors.forename: A L
authors.initials: AL
authors.lastname: Imbembo
authors.forename: K A
authors.initials: KA
authors.lastname: Koehler
mesh_terms: D006801:Humans; D007376:Interleukin-2 / Q000494:pharmacology / Q000502:physiology; D007700:Kinetics; D008561:Membrane Fusion / Q000187:drug effects; D008563:Membrane Lipids / Q000378:metabolism; D008956:Models, Chemical; D010743:Phospholipids / Q000378:metabolism; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000494:pharmacology; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D014364:Tryptophan
chemical_list: D007376:Interleukin-2; D008563:Membrane Lipids; D010743:Phospholipids; D011994:Recombinant Proteins; D014364:Tryptophan