Abstract
Abstract A large collection of Triticum tauschii accessions was previously characterised according to their high and low molecular weight glutenin subunit composition. As a result, one accession was identified as having a subunit with unusual electrophoretic mobility in SDS-PAGE (sodium dodecyl sulphate-polyacrylamide gel electrophoresis). This paper describes further analyses of this protein, named 12.4t. RP-HPLC (reversed phase-high performance liquid chromatography) studies enabled this protein to be classified as a high molecular weight (HMV) glutenin subunit of relatively low molecular weight. A more detailed characterisation of this protein by N-terminal sequence analysis was performed, as well as the molecular characterisation of its encoding gene. Deletions of blocks of the repetitive motifs, probably caused by unequal crossing-over, may have given rise to this particularly small y-type HMW glutenin subunit.
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