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. 2000 Feb 1;345(Pt 3):467–472.

alpha-crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase.

E Ganea 1, J J Harding 1
PMCID: PMC1220779  PMID: 10642503

Abstract

alpha-Crystallin, a major lens protein, has many of the properties of a molecular chaperone, but its ability to assist refolding of proteins has been less certain. In the present work it was shown that alpha-crystallin specifically increased the reactivation of guanidine-denatured glyceraldehyde-3-phosphate dehydrogenase with most of the activity being recovered. In the incubation mixture the recovered enzyme activity was partly free but mostly it appeared in a protective complex with alpha-crystallin. The aggregation of the denatured enzyme on dilution from the guanidine solution was prevented. Thus alpha-crystallin not only protects against aggregation and inactivation of enzymes during denaturation, but can also prevent aggregation and assist recovery of the native structure during renaturation.

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Selected References

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