Interleukin-2 self-association

Biochem Biophys Res Commun. 1988 Apr 29;152(2):879-85. doi: 10.1016/s0006-291x(88)80121-9.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Humans
  • Interleukin-2* / pharmacology
  • Interleukin-2* / physiology
  • Kinetics
  • Membrane Fusion / drug effects
  • Membrane Lipids / metabolism
  • Models, Chemical*
  • Phospholipids / metabolism
  • Protein Conformation
  • Recombinant Proteins / pharmacology
  • Spectrometry, Fluorescence
  • Structure-Activity Relationship
  • Tryptophan

Substances

  • Interleukin-2
  • Membrane Lipids
  • Phospholipids
  • Recombinant Proteins
  • Tryptophan