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J. Biol. Chem., Vol. 269, Issue 40, 24550-24552, 10, 1994
H Cai, CC Wang and CL Tsou
D-Glyceraldehyde-3-phosphate dehydrogenase (GAP-DH) is a protein containing
no disulfide bonds; the guanidine HCl-denatured enzyme shows only a limited
extent of refolding and reactivation upon dilution, and the enzyme is
particularly prone to aggregation during the dilution process. With
increasing GAPDH concentration, reactivation decreases and aggregation
increases. The presence of protein disulfide isomerase in the dilution
mixture markedly increases reactivation of GAPDH and at the same time
prevents the aggregation of GAPDH as shown by light- scattering
measurements. It is suggested that upon dilution, denatured GAPDH is faced
with two competing processes of correct folding and assembly to yield the
native enzyme and non-productive association of the partially refolded
species to form aggregates. Independent of the isomerase activity as no
disulfide bond is present in GAPDH, protein disulfide isomerase assists the
refolding of GAPDH to its active state by suppressing aggregation in a way
closely similar to the action of chaperones.
Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
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