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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Humans
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Interleukin-2* / pharmacology
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Interleukin-2* / physiology
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Kinetics
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Membrane Fusion / drug effects
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Membrane Lipids / metabolism
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Models, Chemical*
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Phospholipids / metabolism
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Protein Conformation
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Recombinant Proteins / pharmacology
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Spectrometry, Fluorescence
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Structure-Activity Relationship
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Tryptophan
Substances
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Interleukin-2
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Membrane Lipids
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Phospholipids
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Recombinant Proteins
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Tryptophan