title: alpha-crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase.
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.
authors.affiliation: Institute of Biochemistry, Splaiul Independentei 296, sect 6, 77700 Bucharest, Romania.
authors.forename: E
authors.initials: E
authors.lastname: Ganea
authors.forename: J J
authors.initials: JJ
authors.lastname: Harding
mesh_terms: D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003459:Crystallins / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D004789:Enzyme Activation; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D019791:Guanidine / Q000737:chemistry / Q000494:pharmacology; D020673:Protein Renaturation
chemical_list: D003459:Crystallins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D019791:Guanidine