PMID: 9650083Jul 3, 1998Paper

Environmental factors influencing the chaperone-like activity of alpha-crystallin

International Journal of Biological Macromolecules
J F KoretzJ N LaButti

Abstract

The effects of mild environmental changes (e.g. the addition of divalent cations or EDTA, as well as variations of buffer pH) on the heat stability and chaperone-like activity of native alpha-crystallin, and denatured-renatured alpha-crystallin in the native molar isoform ratio, have been investigated using circular dichroism (CD) spectropolarimetry and functional assays. The presence or absence of divalent cations has little or no effect on the secondary structure of renatured samples, although chaperone-like activity levels can vary widely; the only relevant spectral difference observed is a loss of some alpha-helical content in all the renatured samples relative to the native protein, but this change has no impact on function. The range of concentration over which the inhibitory Mg2+ effect is observed is 10-fold higher for dialyzed fresh protein than for protein renatured into buffers containing Mg2+, but for both sets of samples, the full effect is established below physiological Mg2+ concentrations. Renaturing into various pH buffers, in contrast, affects both heat stability and chaperone-like activity below pH 7.0, with essentially no functionality observed at pH 6.0. CD spectra of these samples indicate that acidic cond...Continue Reading

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Citations

Feb 19, 2000·Current Opinion in Structural Biology·J I Clark, P J Muchowski
May 12, 2004·Analytical Biochemistry·Andrey S KlymchenkoAlexander P Demchenko
Nov 18, 2011·The Journal of Biological Chemistry·Andi MainzBernd Reif
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Jul 17, 1999·Analytical Chemistry·C K LariveS Bogdanowich-Knipp

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