Activities of superoxide dismutase and glutathione peroxidase in leaves of different cultivars of Liriope spicata L. on 10% SDS-PAGE gels

Activities of superoxide dismutase (SOD) and glutathione peroxidase (GPx) in leaf crude extracts of different cultivars (small leaf, SL; big leaf, BL; thin leaf, TL) of Liriope spicata L. were detected on 10% SDS-PAGE gels. All cultivars contained different Cu/Zn SOD isozymes with molecular masses between 30 and 50 kDa, which were identified by inhibitor tests. They also contained different GPx isozymes with molecular masses between 50 and 64 kDa. It was found that SOD isozymes were stable during 40 to 65°C treatment; however, no SOD activity could be detected at either 70 or 80°C for 5 min. In contrast, all GPx isozymes were stable under 80°C for 5 min, and GPx in SL and TL cultivars could resist 80°C treatment for 30 min.