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Effect of Conformation of Bovine Serum Albumin on Reaction with Its Antibody

From the Laboratory of Immunology, St. Jude Children's Research Hospital, and University of Tennessee, Memphis, Tennessee

Abstract

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 s⁰_20,w of 4.6 S, an expanded molecule with Stokes radius of 20.2 mµ and s⁰_20,w of 1.85 S, and aggregated species having a Stokes radius of 20.2 mµ and s⁰_20,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.

Footnotes

¹ Present address: Department of Histology, Faculty of Medicine, Paraguay 2155, Piso 10, Buenos Aires, Argentina.