A REAGENT FOR REDUCTION OF DISULFIDE BONDS IN PROTEINS THAT REDUCES DISULFIDE BONDS FASTER THAN DOES DITHIOTHREITOL

We have synthesized a new reagent―N,N'-dimethyl-N,N'-bis(mercaptoacetyl)hydrazine (DMH)―for the reduction of disulfide bonds in proteins. DMH reduces disulfide bonds 7 times faster than does dithiothreitol (DTT) in water at pH7. DMH reduces mixed disulfides of cystein proteases (papain and ficin) especially rapdily (30 times faster than DTT). DMH (e o =−0.300 V) reduces moncyclic disulfides completely, although it is less strongly reducing than DTT (e o =−0.356 V)