Protein crosslinking reagents containing a selenoethylene linker are cleaved by mild oxidation.

A homobifunctional cleavable crosslinking reagent containing a selenoethylene group in the linker, and related reagents, have been synthesized and tested in a model system involving formation of a complex between albumin and cytochrome c. Functionally, complex formation was suggested by albumin inhibition of the ascorbate reduction of cytochrome c. Structurally, complex formation was demonstrated by crosslinking and subsequent separation of crosslinked complex from non-crosslinked proteins by SDS-polyacrylamide gel electrophoresis. The crosslinks were found to be cleavable by mild oxidation with low concentrations of periodate or with N-chlorobenzenesulfonamide immobilized on polystyrene beads (Iodo-Beads).