Abstract
Calf lens αA-crystallin isolated by reversed-phase HPLC demonstrates a slightly more hydrophobic profile than αB-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 αA-crystallin than to αB-crystallin at room temperature. Bis-ANS binding to both αA- and αB-crystallin decreases with increase in temperature. At room temperature, the chaperone-like activity of αA-crystallin is lower than that of αB-crystallin whereas at higher temperatures, αA-crystallin shows significantly higher protection against aggregation of substrate proteins compared to αB-crystallin. Therefore, calf lens αA-crystallin is more hydrophobic than αB-crystallin and chaperone-like activity of α-crystallin subunits is not quantitatively related to their hydrophobicity.
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Bhattacharyya, J., Srinivas, V. & Sharma, K.K. Evaluation of Hydrophobicity Versus Chaperonelike Activity of Bovine αA- and αB-Crystallin. J Protein Chem 21, 65–71 (2002). https://doi.org/10.1023/A:1014187300930
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DOI: https://doi.org/10.1023/A:1014187300930