Abstract. In this study reserve endosperm proteins, hordeins of seven spring barley cultivars with different origin: Zernogradskii (Russia), Bodega, Fink, Scarlett and Barke (Germany), Josefin and Astoria (France)
were fractionated and characterized by SDS-PAGE electrophoresis. On the basis of the obtained spectra 19 bands (D + C + B) with different relative electrophoretic mobility and intensity were identified. The electrophoresis profiles of the groups D-, C-and Bhordein are designated as separate types (models) using the index corresponding to hordein blocks. We have established one profile type for D-hordein (D1), two-for C-hordein (C1, C2), and five -for B-hordein (B1, B2, B3, B4, B5). Based on these results hordein formulas (configurations) of accessions are constructed, which enable the expression of specific varietal characteristics and prove the existence of the inter allelic variation (hordein polymorphism) due to the presence or absence of protein components and their different electrophoretic mobility in the profiles of D-, C-and B-hordein.Keywords: spring barley, storage proteins, hordein types, intervarietal polymorphism, SDS-PAGE AGRICULTURAL SCIENCE AND TECHNOLOGY, VOL. 9, No 4, pp 273 -276, 2017 DOI: 10.15547/ast.2017
IntroductionThe use of biochemical markers of genetic control of useful traits is increasingly used in the breeding of barley (Jones, 1982; Hauser et al., 1982;Stoyanova and Popova, 2002). As a result of long research it was found, that electrophoretic spectra of reserve proteins in barley -hordeins -remain unchanged under the influence of environmental conditions (Konarev, 1983(Konarev, , 1983a. Studying the genetic nature of the traits in barley varieties on the basis of polymorphism of reserve proteins is a guarantee for a successful breeding programme (Konarev et al., 1986). The determination of reserve proteins is widely used in studies of plant populations, since variability in their characteristics is genetically determined. They are characterized by a high level of polymorphism and stability.Barley storage proteins -hordeins -have been divided into three groups on the basis of their electrophoretical mobility and amino acid composition (Shewry and Milfin, 1985). D-hordeins have the highest molecular weight (105 kD); they are characterized by a high amino acid (glutamine, glicine and proline) content (Shewry and Tatham, 1990). Synthesis of these hordeins is encoded by the Hor 3 locus located on the long arm of chromosome 1H(5) (Kreis et al., 1984). C-hordeins (50-80 kD), rich in glutamine, phenylalanine and proline, and the major B-hordeins (36-45 kD), rich in glutamine, are encoded by the Hor 1 and Hor 2 loci, respectively, both located on the short arm of chromosome 1H(5) (Shewry and Milfin, 1985). The advantages of hordeins for studying the genetic diversity in barley have been described by many authors (Pomortsev et. al., 2002;Vyhnanek et al., 2003). The barley storage protein hordein is characterized by a high level of polymorphism (Dimova, 2011;Mihova et al., 2...