Abstract
The aggregation and dissociation behavior of bovine α-crystallin as well as the folding and unfolding of its subunits were investigated by equilibrium studies using tryptophan fluorescence measurements and two isoelectric focusing techniques, viz. isoelectric focusing across a urea gradient and isoelectric focusing in two dimensions with different concentrations of urea. It was found that the αB chains lose their ability to aggregate and start unfolding at a lower concentration of urea than the αA chains. Equilibrium intermediates were found upon unfolding or refolding of αA subunits, which can be explained by a two-domain organization of these molecules.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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