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, o f protecting beta-C and gamma-C against heat-induced aggregation was studie d by gel permeation high performance liquid chromatography. The activity wa s calculated using a formula based on the changes in the areas under the ch romatographic peaks of these proteins, which appeared well separated. When heat-induced aggregation was studied in the range 22-90 degrees C, beta-C a ppeared more stable than gamma-C. The activity of alpha-C in stabilizing ga mma-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 co uld be useful for studying the effect of drugs with potential anti-cataract activity on heat-induced aggregation of individual lens proteins.