The Electrolytic Reduction of Proteins^*

Abstract

An electrolytic method is described by which proteins such as bovine plasma albumin, lysozyme, wool keratin, ribonuclease, and insulin may be reduced to various extents. It is usually necessary to add small amounts of a thiol compound, which acts as a current carrier. An improved type of "scanning potentiostat" has been employed, which allows the level of reduction to be automatically controlled. The high extent of reduction without the need for denaturants suggests that the difficulties experienced in reducing certain disulfide bonds in proteins are owing to their low reactivity rather than to their molecular inaccessibility.

The effect of electrical stimulation on the action of sulfhydryl reagents in the giant axon of squid; Suggested mechanisms for the role of thiol and disulfide groups in electrically-induced conformational changes

“…The importance of the availability of thiol groups to the functions of excitable membranes has been emphasized by other workers [2,35]. [NEM] mM Furthermore, it is possible that electrolytic reduction of disulfides might be taking place in depolarized membranes, That disulfides can be reduced to thiols electrolytically in peptides [5] and in proteins [3,20] has been known for some time. Such reactions resulting in the transient production of thiol groups might provide a trigger for the rearrangement of disulfides.…”

Reactions catalyzed by minerals. Part III. The mechanism of spontaneous interlamellar polymerizations in aluminosilicates

“…Chemically reduced clays were prepared by treating the oxidized clays with dilute aqueous hydrazine or by the electrochemical method of Leach et al 4 Polyphosphate-treated montmorilloni tes were prepared by adding 0.5% (by wt. of clay) of a polyphosphate (Calgon marketed by ICIANZ Ltd.) in water to a 5% suspension of the required montmorillonite.…”