Electrophoretic Polymorphism of Globulin Proteins and its Association with Nutritional and Physicochemical Traits in Chickpea (Cicer arietinum L.)
DOI:
https://doi.org/10.37134/jsml.vol14.2.10.2026Keywords:
electrophoretic analysis, genetic diversity, genotypes, spectrum, patternAbstract
The aim of the study was to assess the variability and structural features of chickpea globulin proteins across the electrophoretic zones ω, γ, β, and α. The research employed field observations, polyacrylamide gel electrophoresis, densitometric and spectrophotometric analyses, alongside statistical clustering methods. These techniques successfully distinguished four characteristic zones reflecting proteins of varying molecular masses, enabling a comprehensive assessment of intraspecific polymorphism. Our findings revealed that the high-molecular-weight ω-zone exhibits the greatest structural stability, whereas the γ-zone displays the highest variability, indicating the emergence of diverse globulin isoforms. The β-zone, representing the majority of the total protein complex, contained unique marker fractions, while the low-molecular-weight α-zone showed notable intensity variations across specific genotypes. A substantial proportion of the analyzed genotypes demonstrated unique protein fractions, reflecting a high level of genetic heterogeneity while confirming the fundamental structural role of specific, highly recurrent protein spectra. Ultimately, the identification of these distinct protein polymorphism patterns provides a novel, reliable biochemical marker system to accelerate the selection of genetically diverse, structurally resilient, and nutritionally enhanced chickpea cultivars in modern breeding programs.
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