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Interleukin-2 self-association.

J D Fleischmann·D Wentworth·F Valencic·A L Imbembo·K A Koehler
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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.

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HumansInterleukin-2KineticsMembrane FusionMembrane LipidsModels, ChemicalPhospholipidsProtein ConformationRecombinant ProteinsSpectrometry, FluorescenceStructure-Activity RelationshipTryptophanJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.

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J D Fleischmann, D Wentworth, F Valencic, A L Imbembo, K A Koehler. 1988-04-29. Interleukin-2 self-association.. https://doi.org/10.1016/s0006-291x(88)80121-9

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