Co-purification of a heat-stable antioxidant with the superoxide dismutase activity from dried peas

Abstract A heat-stable antioxidant component was observed to co-purify with the superoxide dismutase (SOD) activity from dried peas. The heat-stable component co-purified by size (gel filtration on Sephadex G-75) and by charge (flat-bed isoelectric focusing (IEF) and Rotofor IEF) coincidently with the SOD activity. Throughout the purification procedure the SOD fractions all exhibited heat-stable antioxidant activity. The autoxidation of linoleic acid in the presence of the pea SOD fraction was delayed for more than four weeks. Purified pea SOD may provide a novel protein-bound, thermostable natural oxidant.