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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Published inBiochemical and biophysical research communications Vol. 152; no. 2; pp. 879 - 885
Main Authors Fleischmann, J.D., Wentworth, D., Valencic, F., Imbembo, A.L., Koehler, K.A.
Format Journal Article
LanguageEnglish
Published San Diego, CA Elsevier Inc 29.04.1988
Elsevier
Subjects
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
HEPES
IL-2
TFA
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Summary: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.
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ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(88)80121-9