Senescence-related protease may play an important role in leaf senescence. By improved SDS-Gela-tin-PAGE assay, a 63 ku senescence-related protease (63 SRP) in coriander leaves was identified. Activity of 63 SRP was i...Senescence-related protease may play an important role in leaf senescence. By improved SDS-Gela-tin-PAGE assay, a 63 ku senescence-related protease (63 SRP) in coriander leaves was identified. Activity of 63 SRP was increased in parallel to the advance of coriander leaf senescence, and inhibited by treating the leaf with gibberellic acid, and enhanced by ethylene treatment. The 63 SRP was suggested to be a serine protease based on the fact that its activity was inhibited by the protease inhibitor PMSF. The optimal temperature for the activity of the 70 ku protease was 50°C. The maximal activity was observed at pH 6-9, some activity could be observed on the gel slices incubated at pH 5 or 11. The 63 SRP was partly purified by the way of ammonium sulfate precipitation and then gel slicing after gel elec-trophoresis.展开更多
基金This work was supported by the Joint Sino-Israeli Agricultural Research Fund (Grant No. SIARF2001-04) the National Natural Science Foundation of China (Grant No. 30070535).
文摘Senescence-related protease may play an important role in leaf senescence. By improved SDS-Gela-tin-PAGE assay, a 63 ku senescence-related protease (63 SRP) in coriander leaves was identified. Activity of 63 SRP was increased in parallel to the advance of coriander leaf senescence, and inhibited by treating the leaf with gibberellic acid, and enhanced by ethylene treatment. The 63 SRP was suggested to be a serine protease based on the fact that its activity was inhibited by the protease inhibitor PMSF. The optimal temperature for the activity of the 70 ku protease was 50°C. The maximal activity was observed at pH 6-9, some activity could be observed on the gel slices incubated at pH 5 or 11. The 63 SRP was partly purified by the way of ammonium sulfate precipitation and then gel slicing after gel elec-trophoresis.
