Literature DB >> 3259135

Interleukin-2 self-association.

J D Fleischmann1, D Wentworth, F Valencic, A L Imbembo, K A Koehler.   

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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Year:  1988        PMID： 3259135     DOI： 10.1016/s0006-291x(88)80121-9

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  3 in total

1.  Macromolecular association of ADP-ribosyltransferase and its correlation with enzymic activity.

Authors:  P I Bauer; K G Buki; A Hakam; E Kun
Journal:  Biochem J       Date:  1990-08-15       Impact factor: 3.857

2.  Insufficient (sub-native) helix content in soluble/solid aggregates of recombinant and engineered forms of IL-2 throws light on how aggregated IL-2 is biologically active.

Authors:  Uzma Fatima; Balvinder Singh; Karthikeyan Subramanian; Purnananda Guptasarma
Journal:  Protein J       Date:  2012-10       Impact factor: 2.371

3.  The effect of pH and temperature on the self-association of recombinant human interleukin-2 as studied by equilibrium sedimentation.

Authors:  S J Advant; E H Braswell; C V Kumar; D S Kalonia
Journal:  Pharm Res       Date:  1995-05       Impact factor: 4.200
  3 in total

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