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  • Title: Inhibition of heat-induced aggregation of beta- and gamma-crystallin by alpha-crystallin evaluated by gel permeation HPLC.
    Author: Saso L, Grippa E, Gatto MT, Leone MG, Silvestrini B.
    Journal: Biochemistry (Mosc); 2000 Feb; 65(2):208-12. PubMed ID: 10713549.
    Abstract:
    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.
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