Studies on the Cold Insoluble Fraction of Peanut Protein

Abstract

Cold insoluble fraction was found to occur in high concentration in 10% sodium chloride soluble protein of the defatted peanut cotyledon. This fraction was further fractionated and analysed by gel filtration chromatography on a Sephadex G-200 column, disc electrophoresis and agarose electrophoresis.
Purified protein was found to be more concentrated in cold insoluble fraction with considerable homogeneity, and contained only two subunit in electrophoretic analysis.