dc.description.abstract | Gluten proteins are formed from proteins of flour, gliadin and glutenins which in contact with
water, begin to interact through the formation of chemical bonds. The aim of this study is
identification of encoding genes polymorphisms of gliadin and glutenins in 10 bread wheat
genotypes. For analysis used 30 seeds of 10 wheat genotypes for extraction of gliadins by
70% ethanole, and glutenins by 10% β-mercaptoethanol.The gliadins were separated by acid
page electrophoresis (pH=3.1) on 8.33% polyacrylamide gel, while glutenins were separated
by SDS-PAGE (pH-8.6) on 11.8% gel. Electrophoregrams were used for determining Gli-1
and Gli-2 alleles. The three alleles (a, b, m) at the Gli-A1, four alleles (b, g, l, k) at the Gli-
B1, five alleles (a, b, f, g, k) at the Gli-D1, five alleles (b, e, f, g, k) at the Gli-A2, four alleles
(b, h, j, p) at the Gli-B2 and three alleles (a, b, r) at the Gli-D2 locus were identified. For high
molecular weight glutenin subunists (HMWGS) the three alleles (a, b, c) at the Glu-A1, three
alleles (b, c, d) at the Glu-B1 and two alleles (a, d) at the Glu-D1 were identified. Gluten
proteins varied according to composition alleles encoding gliadin and glutenins in analyzed
wheat genotypes what related with established polymorphisms of each gliadin and glutenin
loci. | sr |