Physicochemical and immunochemical studies on the reaction of bovine serum albumin with p,p'-difluoro-m,m'-dinitrodiphenylsulfone

Abstract

Bovine serum albumin (BSA) was reacted with the bifunctional reagent p,p'-difluoro-m,m'-dinitrodiphenylsulfone (FNPS) under varying conditions. While intramolecular cross linkages involving the lysine and tyrosine residues were the major modifications, formation of intermolecular linkages (dimerization), favored by high protein concentrations, was observed under all conditions studied. The modified derivatives exhibited decreased precipitin reactions with the antiserum prepared against the native protein indicating that the protein was denatured to some extent during the modification. FNPS appears useful as a general reagent for conjugation of two proteins.