The chaperone activity of bovine alpha crystallin. Interaction with other lens crystallins in native and denatured states.

@article{Wang1994TheCA,
  title={The chaperone activity of bovine alpha crystallin. Interaction with other lens crystallins in native and denatured states.},
  author={Keyang Wang and Abraham Spector},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 18},
  pages={13601-8}
}
It has previously been reported that alpha crystallin (alpha) a major lens protein composed of alpha A and alpha B subunits, can act as a chaperone interacting with other proteins to prevent heat-induced insolubilization. It is now shown that with gamma (gamma), beta L (beta L), and beta H (beta H), other major crystallin groups, this interaction occurs exclusively with soluble denatured protein. Based on studies primarily conducted with the gamma and the beta L crystallins, there is at least… CONTINUE READING

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