Abstract
Calf lens alphaA-crystallin isolated by reversed-phase HPLC demonstrates a slightly more hydrophobic profile than alphaB-crystallin. Fluorescent probes in addition to bis-ANS, like cis-parinaric acid (PA) and pyrene, show higher quantum yields or Ham ratios when bound to alphaA-crystallin than to alphaB-crystallin at room temperature. Bis-ANS binding to both alphaA- and alphaB-crystallin decreases with increase in temperature. At room temperature, the chaperone-like activity of alphaA-crystallin is lower than that of alphaB-crystallin whereas at higher temperatures, alphaA-crystallin shows significantly higher protection against aggregation of substrate proteins compared to alphaB-crystallin. Therefore, calf lens alphaA-crystallin is more hydrophobic than alphaB-crystallin and chaperone-like activity of alpha-crystallin subunits is not quantitatively related to their hydrophobicity.
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