STORAGE-PROTEIN VARIATION IN WILD EMMER WHEAT (TRITICUM-TURGIDUM SSP DICOCCOIDES) FROM JORDAN AND TURKEY .1. ELECTROPHORETIC CHARACTERIZATION OF GENOTYPES

Citation
M. Ciaffi et al., STORAGE-PROTEIN VARIATION IN WILD EMMER WHEAT (TRITICUM-TURGIDUM SSP DICOCCOIDES) FROM JORDAN AND TURKEY .1. ELECTROPHORETIC CHARACTERIZATION OF GENOTYPES, Theoretical and Applied Genetics, 86(4), 1993, pp. 474-480
Citations number
34
Categorie Soggetti
Genetics & Heredity
ISSN journal
00405752
Volume
86
Issue
4
Year of publication
1993
Pages
474 - 480
Database
ISI
SICI code
0040-5752(1993)86:4<474:SVIWEW>2.0.ZU;2-C
Abstract
Seed storage-protein variation at the Glu-A1, Glu-B1 and Gli-B1/Glu-B3 loci in the tetraploid wild progenitor of wheat, T dicoccoides, was s tudied electrophoretically in 315 individuals representing nine popula tions from Jordan and three from Turkey. A total of 44 different HMW-g lutenin patterns were identified, resulting from the combination of 15 alleles in the A genome and 19 in the B genome. Twenty-seven new alle lic variants, 12 at the Glu-A1 locus and 15 at the Glu-B1 locus, were identified by comparing the mobilities of their subunits to those prev iously found in bread and durum wheats. The novel variants include six alleles at the Glu-A1 locus showing both x and y subunits. The genes coding for the 1 Bx and 1 By subunits showed no or very little (3 %) i nactivity, the 1 Ax gene showed a moderate degree (6.3 %) of inactivit y whereas the gene coding for 1 Ay showed the highest degree of inacti vity (84.8 %). A high level of polymorphism was also present for the o mega- and gamma-gliadins and LMW-glutenin subunits encoded by genes at the linked Gli-B1 and Glu-B3 loci (19 alleles). Some Jordanian access ions were found to contain omega-gliadin 35, gamma-gliadin 45, and LMW -2 also present in cultivated durum wheats and related to good gluten viscoelasticity. The newly-discovered alleles enhance the genetic vari ability available for improving the technological quality of wheats. A dditionally some of them may facilitate basic research on the relation ship between industrial properties and the number and functionality of HMW- and LMW-glutenin subunits.