Journal
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
Volume 18, Issue 1, Pages 47-53Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/1475636021000049212
Keywords
protein disulfide isomerase; guanidine hydrochloride; enzyme inhibition; protein folding; interleukin 2
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Initial velocity enzyme kinetics was used to study the inhibition mechanism of guanidine hydrochloride (Gdm.Cl) on catalytic activity of recombinant human protein disulfide isomerase (rhPDI) in protein folding. Reduced C125A recombinant human interleukin 2 (C125A rhIL-2), the substrate, was dissolved in 8 M Gdm.Cl before it was diluted into the folding buffer to initiate the folding reactions. The final Gdm.Cl concentrations in the folding buffer were fixed at 0.2 M, 0.4 M, 0.6 M and 0.8 M. The reduced and native C125A rhIL-2 were resolved by reversed phase-high performance liquid chromatography (RP-HPLC). The simultaneous nonlinear fitting of the initial velocities of the native C125A rhIL-2 formation vs the reduced C125A rhIL-2 concentrations in the presence of different Gdm.Cl concentrations shows that the inhibition mechanism of Gdm.Cl on the catalytic activities of rhPDI is a mixed-type noncompetitive nonlinear inhibition.
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