Demonstration of superoxide dismutase enzymes in extracts of pollen and anther ofzea maysand in two related products, baxtin® and polbax®

Abstract

Abstract Superoxid dismutase enzymes were isolated and identified in an aqueous extract of pollen and anthers of Zea mays and in two commercial products, Baxtin® and Polbax®, derived from the same kind of source material. Prior to analysis the samples were purified by adding soluble poly-Nvinylpyrrolidon and precipitated with ammonium sulphate, Gel filtration chromatography using a Superose 12 HR column gave well-resolved and similar elution patterns for the maize extract, Baxtin and Polbax samples. Fractions exhibiting superoxide dismutase activity, determined by direct KO2 assay, were combined, dialysed and evaporated to dryness. The molecular weight of these fractions was approximately 30000 d. These fractions were also analysed by native polyacrylamide gel electrophoresis and stained for superoxide dismutase enzyme activity using nitro blue tetrazolium. The major region of superoxide dismutase enzyme activity was inhibited by addition of cyanide and hydrogen peroxide indicating the presence of a copper, zinc superoxide dismutase. Another minor region of enzyme activity, migrating as standard manganese superoxide dismutase and not inhibited by cyanide or hydrogen peroxide, was also detected. The results clearly demonstrated the occurrence of both copper, zinc- and manganese superoxide dismutase enzymes in extracts of pollen and anthers of Zea mays and also in the two related commercial products, Baxtin and Polbax.