Summary
The effects of conformational changes of bovine serum albumin on its ability to interact with antibovine serum albumin have been studied. Controlled scission of the disulfide groups by sulfitolysis was performed. The reaction product was found to be heterogeneous, showing three species: a monomer of Stokes radius 3.7 mµ and s020,w of 4.6 S, an expanded molecule with Stokes radius of 20.2 mµ and s020,w of 1.85 S, and aggregated species having a Stokes radius of 20.2 mµ and s020,w of 15.9 S. Separation of the reaction product on Sephadex column yielded 3.7-mµ and 20.2-mµ species; each exhibited differences in the ability to react with anti-bovine serum albumin antibodies.
- Received April 18, 1966.
- Copyright © 1966 by The American Association of Immunologists, Inc.
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