2. Articole
Permanent URI for this collectionhttps://msuir.usm.md/handle/123456789/13419
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Item Some aspects of the winter wheat photosynthetic apparatus resistance to drought(CEP USM, 2024) Shevchenko, Viktor; Bondarenko, OksanaChanges in pigments and proteins content of chloroplast membranes in winter wheat varieties of different resistance under the influence of a drought were studied. The loss of pigments and main structural proteins was greater in less resistant varieties. It was established that the more resistant varieties differed in the increased content of low molecular weight proteins already in the control. Under the drought effects, the relative content of low molecular weight protective proteins increased. Thus, it is shown that the content of proteins of 36, 21 and 16 kDa can be one of the molecular markers of drought resistance.Item Influenţa tratării pomilor de prun cu SBA Reglalg şi microelemente asupra activităţii aparatului fotosintetic, peroxidazei şi catalazei(CEP USM, 2024-10-07) Gîscă, Alina; Popovici, Ana; Svetlicenco, ValentinaVegetative growth and photosynthesis are the mainstaies of plant vitality, productivity and resilience. Over the course of four years, during the vegetation period, the functionality of the photosynthetic apparatus and the activity of the enzymes peroxidase, polyphenoloxidase and catalase were determined in ontogeny in the leaves of four late varieties of plum. Resulting from the average activity of the enzymes investigated in part, we obtained that it changed differently depending on the environmental conditions, high temperatures, genotype, tree treatments, as well as the differentiated role of each enzyme in the metabolic processes that took place in certain phenophases in the leaves of plum trees of the researched varieties. In all varieties, there were higher values in the version treated with SBA Reglalg and microelements Br, Zn, Mn and Mo. The President variety had higher peroxidase values, Stanley and President varieties of polyphenoloxidase, and Stanley variety of catalase.