Seed proteins of 28 Australian bread wheat cultivars were analysed by gel electrophoresis to indicate variations in the composition of their gliadins and glutenin polypeptides (both low- and high-molecular-weight). Composition was indicated according to allelic blocks of genes for each protein class and for each chromosome involved. Relationships were studied between gluten-protein alleles, pedigrees and dough properties (in the Extensograph). Overall, gliadins and low-molecular-weight (LMW) subunits of glutenin controlled by group 1 chromosomes showed closest relationships with each other. LMW subunits were most highly correlated with dough resistance and extensibility. Gliadins controlled by chromosomes 6A and 6D also had highly significant relationships to dough resistance and extensibility, respectively. Among high-molecular-weight subunits of glutenin, however, only those controlled by chromosome 1B showed a significant relationship with resistance to dough extension.
Gliadin alleles were identified in 100 common wheat cultivars registered and/or grown in Spain during the last 40 years. A very high level of genetic polymorphism was found: in total, 103 allelic variants including one null‐allele were found at the six major Gli loci in the Spanish wheats studied. An average genetic diversity for these six loci was found to be higher (H=0.844) than in any group of wheat cultivars studied previously. Spanish wheats bred in Spain demonstrated even higher genetic diversity (H=0.868), probably because of the occurrence in this group of some landraces (local varieties) assumed to be strongly differentiated to fit local environments. The high level of genetic diversity of wheats grown in Spain was maintained by the introduction of distantly related wheat germplasm from different sources, especially from Italy and CIMMYT. A slight decrease of genetic diversity in recently registered cultivars might be caused by the excessive introduction of French wheats. Thirteen new alleles found in Spanish wheats were catalogued, including Gli‐D2w which encodes the first Gli‐D2‐controlledγ‐gliadin to be found.
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