Divinyl sulfone as a crosslinking reagent for oligomeric proteins

Abstract

The kinetics of the nucleophilic addition reactions of divinyl sulfone to amino groups of glycine and model proteins was studied in aqueous solution at 30°C. The rate constants for glycine, bovine serum albu-min, and a1-casein were (4.84±0.58)x10­¹, (2.97± 0.31)x10­², and (2.38 ± 0.49)x10­² M­¹s­¹, respectively. Divinyl sulfone was proposed as a crosslinking reagent for the qualitative detection of protein association in solution. The crosslinking capacity of divinyl sulfone was compared to that of 1,3,5-triacryloylhexahydro-s-tri- azine.