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

Biochem J. 2000 Feb 1;345 Pt 3(Pt 3):467-72.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Chromatography, Affinity
  • Chromatography, Gel
  • Crystallins / chemistry
  • Crystallins / metabolism*
  • Crystallins / pharmacology
  • Enzyme Activation
  • Glyceraldehyde-3-Phosphate Dehydrogenases / chemistry
  • Glyceraldehyde-3-Phosphate Dehydrogenases / drug effects
  • Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism*
  • Guanidine / chemistry
  • Guanidine / pharmacology
  • Protein Renaturation*


  • Crystallins
  • Glyceraldehyde-3-Phosphate Dehydrogenases
  • Guanidine