[Oligomerization of water soluble proteins of rabbit crystalline lens under the action of diamide].
The study has examined the effects of the SH-oxidizing agent diamide (Diazane dicarboxylic acid bis-(N,N-dimethyl-amide)) on the water-soluble portion of proteins from rabbit lenses. The dialyzed protein extracts were incubated for 1-1.5 hrs with various concentrations of diamide. Treatments were monitored for alterations in sulphydryl contents, gel filtration and gel electrophoresis profiles of proteins. The response to 2 mM diamide treatment for 1 hr consists of rapid oxidation (up to 40%) of protein-bound sulphydryl groups accompanied by an appearance of polypeptides with apparent molecular weights. The protein with molecular weight of 29 kilodaltons was shown to be involved in cross-linking. The linkages in the dialyzed water-soluble lens polypeptide fraction induced by diamide may be reduced by GSH (10 mM) treatment of protein extract. The main target of oxidative insult induced by diamide in the water-soluble proteins of the lens is probably the superficially localized sulphydryl groups of crystallins. Our observations suggest that the described oxidative system of proteins may be a useful tool for cataract research.
Babizhaev
M A
MA
Men'shikova
E V
EV
Ritov
V B
VB
D000818:Animals; D002386:Cataract / Q000378:metabolism; D002850:Chromatography, Gel; D003459:Crystallins / Q000378:metabolism*; D003958:Diamide / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D010084:Oxidation-Reduction; D011817:Rabbits; D012106:Research
D003459:Crystallins; D003958:Diamide
Oligomerizatsiia vodorastvorimykh belkov khrustalika krolika pod deĭstviem diamida.