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J. Biol. Chem., Vol. 265, Issue 16, 9114-9120, 06, 1990
J Lundstrom and A Holmgren
We have demonstrated that calf liver protein disulfide-isomerase (Mr
57,000) is a substrate for calf thymus thioredoxin reductase and catalyzes
NADPH-dependent insulin disulfide reduction. This reaction can be used as a
simple assay for protein disulfide-isomerase during purification in place
of the classical method of reactivation of incorrectly oxidized
ribonuclease A. Protein disulfide-isomerase contains two redox-active
disulfides/molecule which were reduced by NADPH and calf thioredoxin
reductase (Km approximately 35 microM). The isomerase was a poor substrate
for NADPH and Escherichia coli thioredoxin reductase, but the addition of
E. coli thioredoxin resulted in rapid reduction of two disulfides/molecule.
Tryptophan fluorescence spectra were shown to monitor the redox state of
protein disulfide- isomerase. Fluorescence measurements demonstrated that
thioredoxin-- (SH)2 reduced the disulfides of the isomerase and allowed the
kinetics of the reaction to be followed; the reaction was also catalyzed by
calf thioredoxin reductase. Equilibrium measurements showed that the
apparent redox potential of the active site disulfide/dithiols of the
thioredoxin domains of protein disulfide-isomerase was about 30 mV higher
than the disulfide/dithiol of E. coli thioredoxin. Consistent with this,
experiments using dithiothreitol or NADPH and thioredoxin
reductase-dependent reduction and precipitation of insulin demonstrated
differences between protein disulfide-isomerase and thioredoxin,
thioredoxin being a better disulfide reductase but less efficient
isomerase. Protein disulfide-isomerase is thus a high molecular weight
member of the thioredoxin system, able to interact with both mammalian
NADPH-thioredoxin reductase and reduced thioredoxin. This may be important
for nascent protein disulfide formation and other thiol- dependent redox
reactions in cells.
Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity
Department of Physiological Chemistry, Karolinska Institutet, Stockholm, Sweden.
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