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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Anilino Naphthalenesulfonates / metabolism
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Animals
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Cattle
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Chromatography, High Pressure Liquid
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Dithiothreitol / metabolism
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Fatty Acids, Unsaturated / chemistry
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Fatty Acids, Unsaturated / metabolism
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Fluorescent Dyes / chemistry
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Fluorescent Dyes / metabolism
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Hydrophobic and Hydrophilic Interactions
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Insulin / metabolism
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Molecular Chaperones / metabolism*
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Pyrenes / chemistry
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Spectrometry, Fluorescence
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Temperature
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alpha-Crystallin A Chain / chemistry*
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alpha-Crystallin A Chain / isolation & purification
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alpha-Crystallin A Chain / metabolism*
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alpha-Crystallin B Chain / chemistry*
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alpha-Crystallin B Chain / isolation & purification
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alpha-Crystallin B Chain / metabolism*
Substances
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Anilino Naphthalenesulfonates
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Fatty Acids, Unsaturated
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Fluorescent Dyes
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Insulin
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Molecular Chaperones
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Pyrenes
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alpha-Crystallin A Chain
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alpha-Crystallin B Chain
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5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate)
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pyrene
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parinaric acid
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Dithiothreitol