Abstract
Abstract Steric exclusion liquid chromatography in the presence of intermediate urea concentrations with lowangle laser light scattering detection was used to investigate the stepwise dissociation of the multimeric bovine eye lens protein α-crystallin. The change in the quaternary structure of α-crystallin as a function of increasing urea concentration clearly resembled dissociation by increasing alkaline pH, urea or guanidine-HC1 concentrations when studied by sedimentation velocity analysis. Next to native and native-like threelayer aggregates (Mr 6.5 − 7.5 × 105), the first dissociation products (two-layer molecules Mr 4 − 5.5 × 105), the second dissociation products (core molecules Mr 2.5 − 3 × 105), and monomeric subunits (Mr 20 000) could be characterized. In the range from 2.6 to 4.4 M urea, we found a gradual decrease in the proportion of the remaining three-layer aggregates and an increase in that of monomeric subunits. The fluorescence emission maxima showed increasing solvent exposure of the tr...
Published Version
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