Abstract:
The present work aims to determine the protein relationship and the physio-biochemical and histo-morphological functions of two tomato varieties (Lycopersicum esculentum Mill var: RioGrand, Heinz) in saline conditions. For this purpose, four factorial experiments were carried out. In a Hoagland solution in a fully randomized block device with four concentrations of NaCl (S0: 0, S1: 25, S2: 50, S3: 150) mMol and four repeats, the work was performed on 32 experimental units for each experiment under controlled conditions. During the germination phase morphological observation showed that the high saline concentration (150 mMol) has a depressive effect on the germination capacity for both varieties. Growth monitoring and seedling development in saline conditions led to the conclusion that salinity significantly decreased the physio-biochemical and morphological parameters (Sf, Psf, Nf,Pft, Bsr, Bsa, Sr, Tre, ChlT, K + r, K + f, Prot) compared to the control against a remarkable accumulation of osmolgulators (Pro, Suc) this consistent with the accretion of the Na+ ion which reflects on the coefficient of selectivity Na + / K + in the leaves and roots of the main component explained (ACP) by the total proteins revealed of very high significant correlations (positive, negative) with the studied parameters this last one seems to have clarified the state of these two varieties (RioGrand, Heinz) in the saline conditions it emerges that these two genotypes showed different behaviors under the high saline concentrations (150 mMol) or we note at the histological study level a structural absence of the growth pri mayor and secondary and an increase in the size of parenchymal cell lignification in the susceptible variety (RioGrand) where the sensitivity index (Is) was confirmed Its sensitivity and an absence of secondary growth in the tolerant variety (Heinz) at the root level this difference lies in the intensity of the bands as well as in the number of bands obtained each band of an
electrophoretic profile composed of several proteins of different structure.
