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. 1997 Dec 1;139(5):1089–1095. doi: 10.1083/jcb.139.5.1089

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Refolding of luciferase by purified chaperones. (a) Chemically denatured luciferase was renatured for 90 min at 25°C in the presence of each chaperone or their combinations. Concentrations of proteins added were: hsc70, 1.8 μM; His-dj2, 0.4 μM; His-dj1, 0.5 μM; DnaJ, 0.5 μM; bovine serum albumin, 1.8 μM. (b) Refolding was performed for indicated periods in the presence of indicated chaperone(s).

Refolding of luciferase by purified chaperones. (a) Chemically denatured luciferase was renatured for 90 min at 25°C in the presence of each chaperone or their combinations. Concentrations of proteins added were: hsc70, 1.8 μM; His-dj2, 0.4 μM; His-dj1, 0.5 μM; DnaJ, 0.5 μM; bovine serum albumin, 1.8 μM. (b) Refolding was performed for indicated periods in the presence of indicated chaperone(s).