Ten proteins were analyzed by potentiometric stripping analysis (PSA)
following reductive accumulation on a HMDE and oxidation with dissolve
d oxygen. During the reductive accumulation period the surface disulfi
de bonds are reduced to sulfhydryl pairs. The rate of oxidation nf the
sulfhydryl pairs is determined by the transport of dissolved oxygen t
o the electrode surface. Comparison of the PSA response to that obtain
ed by constant current chronopotentiometry (CCCP) of the reduced prote
in in a deoxygenated solution showed that the presence of dissolved ox
ygen, in the PSA experiments stabilized the proteins from further conf
ormational changes following the reduction of the surface disulfide bo
nds.