Rotational relaxation of free and protease-bound alpha2-macroglobulin.

@article{Pochon1978RotationalRO,
  title={Rotational relaxation of free and protease-bound alpha2-macroglobulin.},
  author={F Pochon and B Amand and Daniel Lavalette and Joseph G. Bieth},
  journal={The Journal of biological chemistry},
  year={1978},
  volume={253 20},
  pages={7496-9}
}
The recently described triplet probe depolarization technique has been utilized to investigated the rotational relaxation of free and protease-bound alpha2-macroglobulin. The molecular Stokes radius of the free globulin was found to be 88 A, a value which, when compared to the dry radius, indicates a high degree of hydration. The correlation time of alpha2-macroglobulin does not change after its binding with chymotrypsin, but slightly increases in the presence of plasmin. In the presence of 4 M… CONTINUE READING