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Results 1 - 7 of 7
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heterodimeric bacterial luciferase thermally inactivated in the presence of ATPindependent trigger factor is able to refold. In the presence of the DnaKJE chaperone system thermally inactivated heterodimeric bacterial luciferase also refolds
heterodimeric bacterial luciferase thermally inactivated in the presence of ATPindependent trigger factor is able to refold. In the presence of the DnaKJE chaperone system thermally inactivated heterodimeric bacterial luciferase also refolds; heterodimeric bacterial luciferase thermally inactivated in the presence of ATPindependent trigger factor is able to refold. In the presence of the DnaKJE chaperone system thermally inactivated heterodimeric bacterial luciferase also refolds
in the presence of the DnaKJE chaperone system thermally inactivated monomeric bacterial luciferase refolds. Monomeric bacterial luciferase thermally inactivated in the presence of ATPindependent trigger factor is not able to refold
quick refolding within several min at room temperature or 25°C of thermoinactivated enzyme requires ATP and the DnaK-DnaJ-GrpE-system encoding the Hsp70 chaperone but is independent of chaperone ClpA, 80% activity after reactivation, refolding depends on the Escherichia coli strain used for recombinant expression of the luciferase, overview
slow refolding at room temperature or 35°C of thermoinactivated recominant enzyme requires the DnaK-DnaJ-GrpE-system encoding the Hsp70 chaperone, 7-8% activity after refolding over 10 min, refolding depends on the Escherichia coli strain used for recombinant expression of the luciferase, overview
the functional activity of heat-inactivated enzyme is restored by micromolar concentrations of shortchain alkylresorcinols, while longchain homologues inhibit refolding over a wide concentration range. The preincubation of bacterial cells with longchain alkylresorcinols leads to the dose-dependent stimulation of heat shock protein synthesis
Results 1 - 7 of 7