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.

Inhibition of Heat-Induced Aggregation of beta- and gamma-Crystallin by alpha-Crystallin Evaluated by Gel Permeation HPLC / Saso, Luciano; Grippa, E.; Gatto, M. T.; Leone, M. G.; Silvestrini, Bruno. - In: BIOCHEMISTRY. - ISSN 0006-2979. - n. 2, 65:(2000), pp. 208-212.

Inhibition of Heat-Induced Aggregation of beta- and gamma-Crystallin by alpha-Crystallin Evaluated by Gel Permeation HPLC

SASO, Luciano;SILVESTRINI, Bruno
2000

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.
2000
beta- and gamma-crystallin; alpha-crystallin; HPLC
01 Pubblicazione su rivista::01a Articolo in rivista
Inhibition of Heat-Induced Aggregation of beta- and gamma-Crystallin by alpha-Crystallin Evaluated by Gel Permeation HPLC / Saso, Luciano; Grippa, E.; Gatto, M. T.; Leone, M. G.; Silvestrini, Bruno. - In: BIOCHEMISTRY. - ISSN 0006-2979. - n. 2, 65:(2000), pp. 208-212.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/255065
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