| Literature DB >> 81204 |
F Pochon, B Amand, D Lavalette, J Bieth.
Abstract
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 urea, alpha2-macroglobulin dissociates into subunits and this dissociation does not lead to a release of the bound proteases.Entities:
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Year: 1978 PMID： 81204
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157