Open AccessResearch of protein complex of F3 hybrids chickpea seed
Author(s) -
О. О. Молодченкова,
G. D. Lavrova,
Т. В. Картузова,
L. Ya. Bezkrovna,
O. B. Lykhota,
O. V. Ryshchakova,
Yu. A. Levitsky
Publication year - 2020
Publication title -
faktori eksperimentalʹnoï evolûcìï organìzmìv
Language(s) - English
Resource type - Journals
eISSN - 2415-3826
pISSN - 2219-3782
DOI - 10.7124/feeo.v27.1334
Subject(s) - legumin , vicilin , globulin , hybrid , trypsin inhibitor , trypsin , biology , biochemistry , chemistry , food science , botany , storage protein , gene , enzyme , immunology
Aim. The aim of the study was to investigate the peculiarities of the protein complex of seeds of F3 hybrid populations and their parental forms of chickpea (Cicer arietinum L.) of Ukrainian and foreign breeding. Methods. Research methods are standard methodologies of plant biochemical analysis and methods developed in the laboratory (Kjeldahl method, spectrophotometric methods, protein electrophoresis). Results. The peculiarities of protein content, basic fractions of globulins – legumin and vicilin, activity of trypsin inhibitor, lectins, lipoxygenase in the seeds of F3 hybrid populations and their parent forms of chickpea have been established. It was shown using electrophoretic and densitometric analyses that F3 hybrid populations of chickpea were non identifical in level and character of globulin component composition variability. The clear differences are observed both in the intensity of the staining and the displacement of protein components of legumin and vicilin which are identical in mobility, presence and absence of components that are typical for particular hybrid combination. Conclusions. Obtained results can be used to selection of chickpea genotypes of food direction.
Keywords: chickpea, protein, vicilin, legumin, trypsin inhibitor.