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S Gopalakrishnan, D Boyle, L Takemoto; Preferential interaction of alpha crystallin with denatured forms of gamma crystallin.. Invest. Ophthalmol. Vis. Sci. 1994;35(2):382-387.
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PURPOSE: To characterize the possible interaction of alpha crystallin with partially denatured forms of gamma crystallin. METHODS: Gamma crystallin was denatured in the presence of guanidine hydrochloride, then dialyzed in the presence or absence of alpha crystallin. The high-molecular-weight complex formed in the presence of alpha was characterized by gel filtration chromatography, electron microscopy, and quantitative Western blot analysis. RESULTS: Relative to native alpha or reconstituted aggregates of purified alpha, the higher molecular weight complex possessed a greater mean diameter and contained increased amounts of gamma crystallin. CONCLUSIONS: Alpha crystallin preferentially interacts with partially denatured forms of a lens protein, consistent with its putative role as a functional molecular chaperone in the intact lens.
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