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. 2014 Dec 17;5:5804. doi: 10.1038/ncomms6804

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(a,b) The Drosophila melanogaster RidA homologue DUK114 was purified and subjected to chaperone assays. Inhibition of citrate synthase aggregation strongly depends on the ratio of DUK114_HOCl over citrate synthase similar to RidA_HOCl and other unrelated proteins. (c) In contrast to RidA_HOCl (and β-lactoglobulin; see also f), activation of DUK114_HOCl is only partially reversible by DTT. (d,e) In addition to DUK114, a number of other proteins was tested for HOCl-induced chaperone activity. RNaseA and lipase are unaffected by HOCl treatment, whereas β-lactoglobulin, α-amylase and BSA show HOCl-inducible chaperone activity. BSA is already active before treatment (d). (f) Activation of β-lactoglobulin is reversible by DTT. Representative measurements are shown for a,d,e and f. Data represented in b and c are the means of three independent measurements.