Peanut proteins and enzymes solubilized in the presence of high concentrations of dithiothreitol (DTT) or d-mercaptoethanol (d-ME), then examined by polyacrylamide or starch gel electrophoresis, showed significant changes in their mobilities and activities, respectively, when compared to those of control extracts (without thiol-reducing compounds). Frozen storage altered the solubility characteristics and electrophoretic patterns of these proteins, especially when the samples contained high concentrations of a reducing reagent. These changes were quite noticeable with protein fractions separated from arachin and with enzymes after DEAE-cellulose chromatography.The results indicate that thiol-reducing compounds and/or frozen storage promote many in vitro changes (e.g., molecular weight, conformational, structural, steric hindrance, and functional properties) in extracted peanut proteins and enzymes.Reactive thiol groups have several roles in proteins; e.g., they help to maintain protein conformation and stability