The activity of the peroxidase system in Mesembryanthemum crystallinum L. plants in relation to the shift from C3 to CAM photosynthesis was studied. In detached leaves of the fourth and fifth stories treated with NaCl (0.3 M), a rapid (after 30 min) transient induction of the ionically bound peroxidase (the first maximum) was observed followed by a second weak increase in the enzyme activity (90 min after salt treatment). In the leaves of intact plants, which received a longer treatment with NaCl, a two-phase change in the enzyme activity was also observed. It was most pronounced at the early stages of the NaCl-induced plant shift from C3 to CAM photosynthesis. In this case, in both detached and intact leaves of juvenile plants, the activity of soluble peroxidase was at a low steady-state level. The situation changed dramatically when M. crystallinum plants transitioned to the reproductive developmental phase and photosynthesis switched from C3 to CAM. The time dependence of the activities of both peroxidase types, the soluble ones in particular, was characterized by marked diurnal oscillations (light–dark), which coincided with the fluctuations of the total titratable acidity. In this case, the activity of the soluble enzyme was several orders of magnitude higher than the activity of the ionically bound peroxidase, even though the optimum pH for both isoforms was similar (pH 5.0). Three acid isoforms of soluble peroxidases, which operated more actively when the cytoplasm had a higher acidity, were distinguished by isoelectrofocusing. Their activity increased under salinity. Alkaline and neutral components were predominant in more than 30 molecular forms of the soluble peroxidase detected. We concluded that the operation of the peroxidase system changed substantially when plants shifted from the juvenile to the reproductive state and switched from C3 to CAM photosynthesis: the activity of stress-induced ionically bound peroxidase was drastically inhibited with a concurrent increase in the activity of soluble peroxidase and a change in the spectrum of its molecular forms.
Russian Journal of Plant Physiology – Springer Journals
Published: Oct 13, 2004
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