Interleukin-2 self-association

The self-association of human recombinant interleukin-2 (IL-2) from E. coli was explored. Self-association, with an apparent K d 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 apparen...

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Veröffentlicht in:	Biochemical and biophysical research communications 1988-04, Vol.152 (2), p.879-885
Hauptverfasser:	Fleischmann, J.D., Wentworth, D., Valencic, F., Imbembo, A.L., Koehler, K.A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences Fundamental and applied biological sciences. Psychology Fundamental immunology 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
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Beschreibung
Zusammenfassung:	The self-association of human recombinant interleukin-2 (IL-2) from E. coli was explored. Self-association, with an apparent K d 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.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/S0006-291X(88)80121-9