Study of the chaperoning mechanism of bovine lens alpha-crystallin, a member of the alpha-small heat shock superfamily.

@article{Abgar2001StudyOT,
  title={Study of the chaperoning mechanism of bovine lens alpha-crystallin, a member of the alpha-small heat shock superfamily.},
  author={Saı¨d Abgar and Jos Vanhoudt and Thierry Aerts and Julius Clauwaert},
  journal={Biophysical journal},
  year={2001},
  volume={80 4},
  pages={
          1986-95
        }
}
We have studied the interaction between lysozyme, destabilized by reducing its -S-S- bonds, and bovine eye lens alpha-crystallin, a member of the alpha-small heat shock protein superfamily. We have used gel filtration, photon correlation spectroscopy, and analytical ultracentrifugation to study the binding of lysozyme by alpha-crystallin at 25 degrees C and 37 degrees C. We can conclude that alpha-crystallin chaperones the destabilized protein in a two-step process. First the destabilized… CONTINUE READING

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