Prevention of the fructation-induced inactivation of glutathione reductase by bovine alpha-crystallin acting as a molecular chaperone.
We had previously shown that glutathione reductase was inactivated by glycation, and decided to use this model system to see whether bovine alpha-crystallin could provide protection, and whether its modification had an effect. Other proteins were used as a comparison. Both forms of alpha-crystallin prevented loss of enzyme activity on incubation with fructose. No such protection was profferred by the other proteins, suggesting bovine alpha-crystallin acted in a chaperone-like manner.
Blakytny
R
R
Nuffield Laboratory of Ophthalmology, Oxford University, UK.
Harding
J J
JJ
D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000502:physiology*; D005632:Fructose / Q000378:metabolism; D005980:Glutathione Reductase / Q000737:chemistry / Q000378:metabolism*; D018832:Molecular Chaperones; D011499:Protein Processing, Post-Translational
D003459:Crystallins; D018832:Molecular Chaperones; D005632:Fructose; D005980:Glutathione Reductase