Evaluation of hydrophobicity versus chaperonelike activity of bovine alphaA- and alphaB-crystallin

Journal of Protein Chemistry
Jaya BhattacharyyaK Krishna Sharma

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.

Citations

Dec 15, 2010·International Journal of Molecular Sciences·Zoya BumaginaBoris Kurganov
Nov 7, 2006·IUBMB Life·G Bhanuprakash ReddyM Satish Kumar
Nov 1, 2006·Protein Science : a Publication of the Protein Society·Puttur Santhoshkumar, K Krishna Sharma
Feb 14, 2019·Biochemistry·Sandip K NandiRam H Nagaraj
Dec 15, 2004·Biochemistry·Yellamaraju SreelakshmiK Krishna Sharma

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