Inhibition of heat-induced aggregation of beta- and gamma-crystallin by alpha-crystallin evaluated by gel permeation HPLC.
The capability of alpha-crystallin (alpha-C), a known molecular chaperon, of protecting beta-C and gamma-C against heat-induced aggregation was studied by gel permeation high performance liquid chromatography. The activity was calculated using a formula based on the changes in the areas under the chromatographic peaks of these proteins, which appeared well separated. When heat-induced aggregation was studied in the range 22-90 degrees C, beta-C appeared more stable than gamma-C. The activity of alpha-C in stabilizing gamma-C but not beta-C was already relevant at 60 degrees C, but the maximum activity was higher (about 35%) for beta-C than for gamma-C. This method could be useful for studying the effect of drugs with potential anti-cataract activity on heat-induced aggregation of individual lens proteins.
Saso
L
L
Department of Pharmacology of Natural Substances and General Physiology, University of Rome "La Sapienza", Rome, 00185, Italy.
Grippa
E
E
Gatto
M T
MT
Leone
M G
MG
Silvestrini
B
B
D002386:Cataract / Q000188:drug therapy / Q000378:metabolism / Q000517:prevention & control; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D003459:Crystallins / Q000737:chemistry* / Q000187:drug effects / Q000494:pharmacology*; D004355:Drug Stability; D006358:Hot Temperature; D006801:Humans; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D018832:Molecular Chaperones / Q000494:pharmacology; D011489:Protein Denaturation / Q000187:drug effects
D003459:Crystallins; D046911:Macromolecular Substances; D018832:Molecular Chaperones